Cysteine proteinase found in many tissues. Hydrolyzes a variety of endogenous proteins including NEUROPEPTIDES; CYTOSKELETAL PROTEINS; proteins from SMOOTH MUSCLE; CARDIAC MUSCLE; liver; platelets; and erythrocytes. Two subclasses having high and low calcium sensitivity are known. Removes Z-discs and M-lines from myofibrils. Activates phosphorylase kinase and cyclic nucleotide-independent protein kinase. This enzyme was formerly listed as EC 3.4.22.4.
An adenine nucleotide containing three phosphate groups esterified to the sugar moiety. In addition to its crucial roles in metabolism adenosine triphosphate is a neurotransmitter.
A group of enzymes which catalyze the hydrolysis of ATP. The hydrolysis reaction is usually coupled with another function such as transporting Ca(2+) across a membrane. These enzymes may be dependent on Ca(2+), Mg(2+), anions, H+, or DNA.
A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.
Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group include EXOPEPTIDASES and ENDOPEPTIDASES.
The rate dynamics in chemical or physical systems.
A basic element found in nearly all organized tissues. It is a member of the alkaline earth family of metals with the atomic symbol Ca, atomic number 20, and atomic weight 40. Calcium is the most abundant mineral in the body and combines with phosphorus to form calcium phosphate in the bones and teeth. It is essential for the normal functioning of nerves and muscles and plays a role in blood coagulation (as factor IV) and in many enzymatic processes.
Non-nucleated disk-shaped cells formed in the megakaryocyte and found in the blood of all mammals. They are mainly involved in blood coagulation.
The sum of the weight of all the atoms in a molecule.
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme.
Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES).
Enzyme of the human immunodeficiency virus that is required for post-translational cleavage of gag and gag-pol precursor polyproteins into functional products needed for viral assembly. HIV protease is an aspartic protease encoded by the amino terminus of the pol gene.
Any member of the group of ENDOPEPTIDASES containing at the active site a serine residue involved in catalysis.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
A prokaryotic ATP-dependent protease that plays a role in the degradation of many abnormal proteins. It is a tetramer of 87-kDa subunits, each of which contains a proteolytic site and a ATP-binding site.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
A subclass of peptide hydrolases that depend on a CYSTEINE residue for their activity.
Proteases that contain proteolytic core domains and ATPase-containing regulatory domains. They are usually comprised of large multi-subunit assemblies. The domains can occur within a single peptide chain or on distinct subunits.
ENDOPEPTIDASES which have a cysteine involved in the catalytic process. This group of enzymes is inactivated by CYSTEINE PROTEINASE INHIBITORS such as CYSTATINS and SULFHYDRYL REAGENTS.
Extracellular protease inhibitors that are secreted from FIBROBLASTS. They form a covalent complex with SERINE PROTEASES and can mediate their cellular internalization and degradation.
Exogenous or endogenous compounds which inhibit SERINE ENDOPEPTIDASES.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
The process of cleaving a chemical compound by the addition of a molecule of water.
Established cell cultures that have the potential to propagate indefinitely.
Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.
Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.
Proteins prepared by recombinant DNA technology.
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway.
Proteins found in any species of bacterium.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
Exogenous and endogenous compounds which inhibit CYSTEINE ENDOPEPTIDASES.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
A group of lysosomal proteinases or endopeptidases found in aqueous extracts of a variety of animal tissues. They function optimally within an acidic pH range. The cathepsins occur as a variety of enzyme subtypes including SERINE PROTEASES; ASPARTIC PROTEINASES; and CYSTEINE PROTEASES.
Adenosine 5'-(trihydrogen diphosphate). An adenine nucleotide containing two phosphate groups esterified to the sugar moiety at the 5'-position.
The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.
Elements of limited time intervals, contributing to particular results or situations.
A serine endopeptidase that is formed from TRYPSINOGEN in the pancreas. It is converted into its active form by ENTEROPEPTIDASE in the small intestine. It catalyzes hydrolysis of the carboxyl group of either arginine or lysine. EC 3.4.21.4.
Multisubunit enzyme complexes that synthesize ADENOSINE TRIPHOSPHATE from energy sources such as ions traveling through channels.
Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility.
Members of the peptidase C19 family which regulate signal transduction by removing UBIQUITIN from specific protein substrates via a process known as deubiquitination or deubiquitylation.
An ATP-dependent protease found in prokaryotes, CHLOROPLASTS, and MITOCHONDRIA. It is a soluble multisubunit complex that plays a role in the degradation of many abnormal proteins.
Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.
One of the mechanisms by which CELL DEATH occurs (compare with NECROSIS and AUTOPHAGOCYTOSIS). Apoptosis is the mechanism responsible for the physiological deletion of cells and appears to be intrinsically programmed. It is characterized by distinctive morphologic changes in the nucleus and cytoplasm, chromatin cleavage at regularly spaced sites, and the endonucleolytic cleavage of genomic DNA; (DNA FRAGMENTATION); at internucleosomal sites. This mode of cell death serves as a balance to mitosis in regulating the size of animal tissues and in mediating pathologic processes associated with tumor growth.
The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.
ENDOPEPTIDASES which use a metal such as ZINC in the catalytic mechanism.
A family of SERINE ENDOPEPTIDASES isolated from Bacillus subtilis. EC 3.4.21.-
The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.
RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.
A serine endopeptidase secreted by the pancreas as its zymogen, CHYMOTRYPSINOGEN and carried in the pancreatic juice to the duodenum where it is activated by TRYPSIN. It selectively cleaves aromatic amino acids on the carboxyl side.
Peptides composed of between two and twelve amino acids.
Theoretical representations that simulate the behavior or activity of biological processes or diseases. For disease models in living animals, DISEASE MODELS, ANIMAL is available. Biological models include the use of mathematical equations, computers, and other electronic equipment.
A sub-subclass of endopeptidases that depend on an ASPARTIC ACID residue for their activity.
The relationship between the dose of an administered drug and the response of the organism to the drug.
Transport proteins that carry specific substances in the blood or across cell membranes.
Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes.
Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.
The species Oryctolagus cuniculus, in the family Leporidae, order LAGOMORPHA. Rabbits are born in burrows, furless, and with eyes and ears closed. In contrast with HARES, rabbits have 22 chromosome pairs.
Cleavage of proteins into smaller peptides or amino acids either by PROTEASES or non-enzymatically (e.g., Hydrolysis). It does not include Protein Processing, Post-Translational.
Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.
The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.
N-acylated oligopeptides isolated from culture filtrates of Actinomycetes, which act specifically to inhibit acid proteases such as pepsin and renin.
Semiautonomous, self-reproducing organelles that occur in the cytoplasm of all cells of most, but not all, eukaryotes. Each mitochondrion is surrounded by a double limiting membrane. The inner membrane is highly invaginated, and its projections are called cristae. Mitochondria are the sites of the reactions of oxidative phosphorylation, which result in the formation of ATP. They contain distinctive RIBOSOMES, transfer RNAs (RNA, TRANSFER); AMINO ACYL T RNA SYNTHETASES; and elongation and termination factors. Mitochondria depend upon genes within the nucleus of the cells in which they reside for many essential messenger RNAs (RNA, MESSENGER). Mitochondria are believed to have arisen from aerobic bacteria that established a symbiotic relationship with primitive protoeukaryotes. (King & Stansfield, A Dictionary of Genetics, 4th ed)
Strains of mice in which certain GENES of their GENOMES have been disrupted, or "knocked-out". To produce knockouts, using RECOMBINANT DNA technology, the normal DNA sequence of the gene being studied is altered to prevent synthesis of a normal gene product. Cloned cells in which this DNA alteration is successful are then injected into mouse EMBRYOS to produce chimeric mice. The chimeric mice are then bred to yield a strain in which all the cells of the mouse contain the disrupted gene. Knockout mice are used as EXPERIMENTAL ANIMAL MODELS for diseases (DISEASE MODELS, ANIMAL) and to clarify the functions of the genes.
The property of objects that determines the direction of heat flow when they are placed in direct thermal contact. The temperature is the energy of microscopic motions (vibrational and translational) of the particles of atoms.
Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.
Compounds or agents that combine with an enzyme in such a manner as to prevent the normal substrate-enzyme combination and the catalytic reaction.
A metallic element that has the atomic symbol Mg, atomic number 12, and atomic weight 24.31. It is important for the activity of many enzymes, especially those involved in OXIDATIVE PHOSPHORYLATION.
The uptake of naked or purified DNA by CELLS, usually meaning the process as it occurs in eukaryotic cells. It is analogous to bacterial transformation (TRANSFORMATION, BACTERIAL) and both are routinely employed in GENE TRANSFER TECHNIQUES.
The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.
The biosynthesis of RNA carried out on a template of DNA. The biosynthesis of DNA from an RNA template is called REVERSE TRANSCRIPTION.
Identification of proteins or peptides that have been electrophoretically separated by blot transferring from the electrophoresis gel to strips of nitrocellulose paper, followed by labeling with antibody probes.
Physiologically inactive substances that can be converted to active enzymes.
Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are linear polypeptides that are normally synthesized on RIBOSOMES.
The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups.
Proteins which bind to DNA. The family includes proteins which bind to both double- and single-stranded DNA and also includes specific DNA binding proteins in serum which can be used as markers for malignant diseases.
A family of serine proteinase inhibitors which are similar in amino acid sequence and mechanism of inhibition, but differ in their specificity toward proteolytic enzymes. This family includes alpha 1-antitrypsin, angiotensinogen, ovalbumin, antiplasmin, alpha 1-antichymotrypsin, thyroxine-binding protein, complement 1 inactivators, antithrombin III, heparin cofactor II, plasminogen inactivators, gene Y protein, placental plasminogen activator inhibitor, and barley Z protein. Some members of the serpin family may be substrates rather than inhibitors of SERINE ENDOPEPTIDASES, and some serpins occur in plants where their function is not known.
The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.
Extrachromosomal, usually CIRCULAR DNA molecules that are self-replicating and transferable from one organism to another. They are found in a variety of bacterial, archaeal, fungal, algal, and plant species. They are used in GENETIC ENGINEERING as CLONING VECTORS.
The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.
A protease of broad specificity, obtained from dried pancreas. Molecular weight is approximately 25,000. The enzyme breaks down elastin, the specific protein of elastic fibers, and digests other proteins such as fibrin, hemoglobin, and albumin. EC 3.4.21.36.
Proton-translocating ATPases responsible for ADENOSINE TRIPHOSPHATE synthesis in the MITOCHONDRIA. They derive energy from the respiratory chain-driven reactions that develop high concentrations of protons within the intermembranous space of the mitochondria.
The first continuously cultured human malignant CELL LINE, derived from the cervical carcinoma of Henrietta Lacks. These cells are used for VIRUS CULTIVATION and antitumor drug screening assays.
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control (induction or repression) of gene action at the level of transcription or translation.

Enhanced mitochondrial biogenesis is associated with increased expression of the mitochondrial ATP-dependent Lon protease. (1/362)

Rats bearing the Zajdela hepatoma tumor and T3-treated hypothyroid rats were used to study the role of protein degradation in the process of mitochondrial biogenesis. It was shown that the activity, protein and mRNA levels of the ATP-dependent Lon protease increased in rapidly growing Zajdela hepatoma cells. The increase in the rate of mitochondrial biogenesis by thyroid hormone was similarly accompanied by enhanced expression of the Lon protease. The results imply that mitochondrial biogenesis in mammalian cells is, at least partially, regulated by the matrix Lon protease.  (+info)

A conserved domain in Escherichia coli Lon protease is involved in substrate discriminator activity. (2/362)

Lon protease of Escherichia coli regulates a diverse set of physiological responses including cell division, capsule production, plasmid stability, and phage replication. Little is known about the mechanism of substrate recognition by Lon. To examine the interaction of Lon with two of its substrates, RcsA and SulA, we generated point mutations in lon which affected its substrate specificity. The most informative lon mutant overproduced capsular polysaccharide (RcsA stabilized) yet was resistant to DNA-damaging agents (SulA degraded). Immunoblots revealed that RcsA protein persisted in this mutant whereas SulA protein was rapidly degraded. The mutant contains a single-base change within lon leading to a single amino acid change of glutamate 240 to lysine. E240 is conserved among all Lon isolates and resides in a charged domain that has a high probability of adopting a coiled-coil conformation. This conformation, implicated in mediating protein-protein interactions, appears to confer substrate discriminator activity on Lon. We propose a model suggesting that this coiled-coil domain represents the discriminator site of Lon.  (+info)

Expression of mitochondrial marker proteins during spermatogenesis. (3/362)

Spermatogenesis is a highly complex, hormonally regulated cytodifferentiation process finally leading to the production of spermatozoa. In addition to other events germ cell differentiation is characterized by a gradual structural modification of many organelles including mitochondria which play a unique role. The morphological and functional development of germ cell mitochondria is a reflection of the permanent change in the testicular microenvironment which occurs when the germ cells are slowly moving from the base of the seminiferous epithelium to the lumen. Concomitant with the structural changes, several mitochondrial proteins are known to be expressed and synthesized during distinct phases of the organelle's development. This review pays particular attention to these transiently expressed mitochondrial proteins such as hsp60, Lon protease, sulphydryl oxidase and cytochrome ct. Furthermore, the biological function of this stepwise gene activation during mitochondrial and germ cell development is discussed.  (+info)

Substrate sequestration by a proteolytically inactive Lon mutant. (4/362)

Lon protein of Escherichia coli is an ATP-dependent protease responsible for the rapid turnover of both abnormal and naturally unstable proteins, including SulA, a cell division inhibitor made after DNA damage, and RcsA, a positive regulator of transcription. Lon is a multimer of identical 94-kDa subunits, each containing a consensus ATPase motif and a serine active site. We found that overexpressing Lon, which is mutated for the serine active site (LonS679A) and is therefore devoid of proteolytic activity, unexpectedly led to complementation of the UV sensitivity and capsule overproduction of a lon deletion mutant. SulA was not degraded by LonS679A, but rather was completely protected by the Lon mutant from degradation by other cellular proteases. We interpret these results to mean that the mutant LonS679A binds but does not degrade Lon substrates, resulting in sequestration of the substrate proteins and interference with their activities, resulting in apparent complementation. Lon that carried a mutation in the consensus ATPase site, either with or without the active site serine, was no longer able to complement a Deltalon mutant. These in vivo results suggest that the pathway of degradation by Lon couples ATP-dependent unfolding with movement of the substrate into protected chambers within Lon, where it is held until degradation proceeds. In the absence of degradation the substrate remains sequestered. Comparison of our results with those from a number of other systems suggest that proteins related to the regulatory portions of energy-dependent proteases act as energy-dependent sequestration proteins.  (+info)

Role of region C in regulation of the heat shock gene-specific sigma factor of Escherichia coli, sigma32. (5/362)

Expression of heat shock genes is controlled in Escherichia coli by the antagonistic action of the sigma32 subunit of RNA polymerase and the DnaK chaperone system, which inactivates sigma32 by stress-dependent association and mediates sigma32 degradation by the FtsH protease. A stretch of 23 residues (R122 to Q144) conserved among sigma32 homologs, termed region C, was proposed to play a role in sigma32 degradation, and peptide analysis identified two potential DnaK binding sites central and peripheral to region C. Region C is thus a prime candidate for mediating stress control of sigma32, a hypothesis that we tested in the present study. A peptide comprising the central DnaK binding site was an excellent substrate for FtsH, while a peptide comprising the peripheral DnaK binding site was a poor substrate. Replacement of a single hydrophobic residue in each DnaK binding site by negatively charged residues (I123D and F137E) strongly decreased the binding of the peptides to DnaK and the degradation by FtsH. However, introduction of these and additional region C alterations into the sigma32 protein did not affect sigma32 degradation in vivo and in vitro or DnaK binding in vitro. These findings do not support a role for region C in sigma32 control by DnaK and FtsH. Instead, the sigma32 mutants had reduced affinities for RNA polymerase and decreased transcriptional activities in vitro and in vivo. Furthermore, cysteines inserted into region C allowed cysteine-specific cross-linking of sigma32 to RNA polymerase. Region C thus confers on sigma32 a competitive advantage over other sigma factors to bind RNA polymerase and thereby contributes to the rapidity of the heat shock response.  (+info)

Dislocation of membrane proteins in FtsH-mediated proteolysis. (6/362)

Escherichia coli FtsH degrades several integral membrane proteins, including YccA, having seven transmembrane segments, a cytosolic N-terminus and a periplasmic C-terminus. Evidence indicates that FtsH initiates proteolysis at the N-terminal cytosolic domain. SecY, having 10 transmembrane segments, is also a substrate of FtsH. We studied whether and how the FtsH-catalyzed proteolysis on the cytosolic side continues into the transmembrane and periplasmic regions using chimeric proteins, YccA-(P3)-PhoA-His6-Myc and SecY-(P5)-PhoA, with the alkaline phosphatase (PhoA) mature sequence in a periplasmic domain. The PhoA domain that was present within the fusion protein was rapidly degraded by FtsH when it lacked the DsbA-dependent folding. In contrast, both PhoA itself and the TM9-PhoA region of SecY-(P5)-PhoA were stable when expressed as independent polypeptides. In the presence of DsbA, the FtsH-dependent degradation stopped at a site near to the N-terminus of the PhoA moiety, leaving the PhoA domain (and its C-terminal region) undigested. The efficiency of this degradation stop correlated well with the rapidity of the folding of the PhoA domain. Thus, both transmembrane and periplasmic domains are degraded by the processive proteolysis by FtsH, provided they are not tightly folded. We propose that FtsH dislocates the extracytoplasmic domain of a substrate, probably using its ATPase activity.  (+info)

Lon and Clp family proteases and chaperones share homologous substrate-recognition domains. (7/362)

Lon protease and members of the Clp family of molecular chaperones and protease regulatory subunits contain homologous regions with properties expected for substrate-binding domains. Fragments corresponding to these sequences are stably and independently folded for Lon, ClpA, and ClpY. The corresponding regions from ClpB and ClpX are unstable. All five fragments exhibit distinct patterns of binding to three proteins that are protease substrates in vivo: the heat shock transcription factor sigma32, the SOS mutagenesis protein UmuD, and Arc repressor bearing the SsrA degradation tag. Recognition of UmuD is mediated through peptide sequences within a 24-residue N-terminal region whereas recognition of both sigma32 and SsrA-tagged Arc requires sequences at the C terminus. These results indicate that the Lon and Clp proteases use the same mechanism of substrate discrimination and suggest that these related ATP-dependent bacterial proteases scrutinize accessible or disordered regions of potential substrates for the presence of specific targeting sequences.  (+info)

Mitochondrial Lon of Saccharomyces cerevisiae is a ring-shaped protease with seven flexible subunits. (8/362)

Lon (or La) is a soluble, homooligomeric ATP-dependent protease. Mass determination and cryoelectron microscopy of pure mitochondrial Lon from Saccharomyces cerevisiae identify Lon as a flexible ring-shaped heptamer. In the presence of ATP or 5'-adenylylimidodiphosphate, most of the rings are symmetric and resemble other ATP-driven machines that mediate folding and degradation of proteins. In the absence of nucleotides, most of the rings are distorted, with two adjacent subunits forming leg-like protrusions. These results suggest that asymmetric conformational changes serve to power processive unfolding and translocation of substrates to the active site of the Lon protease.  (+info)

Mitochondria are multifunctional organelles that play a central role in energy metabolism. Owing to the life-essential functions of these organelles, mitochondrial content, quality and dynamics are tightly controlled. Across the species, highly conserved ATP-dependent proteases prevent malfunction of mitochondria through versatile activities. This study focuses on a molecular function of the plant mitochondrial inner membrane-embedded AAA protease (denoted i-AAA) FTSH4, providing its first bona fide substrate. Here, we report that the abundance of the Tim17-2 protein, an essential component of the TIM17:23 translocase (Tim17-2 together with Tim50 and Tim23), is directly controlled by the proteolytic activity of FTSH4. Plants that are lacking functional FTSH4 protease are characterized by significantly enhanced capacity of preprotein import through the TIM17:23-dependent pathway. Taken together, with the observation that FTSH4 prevents accumulation of Tim17-2, our data point towards the role of ...
Purchase Recombinant Shewanella baltica ATP-dependent protease subunit HslV(hslV). It is produced in Yeast. High purity. Good price.
ATP-dependent protease. Molecular model of the bacterial enzyme HsIUV protease. Proteases are enzymes that break down proteins. HsIUV is expressed in response to cellular stress. - Stock Image C025/1906
Introduction - ATP-dependent proteases constitute a unique proteolytic system. Although proteolysis is an exergonic process, these proteases require energy derived from ATP hydrolysis in order to function. This energy requirement is closely related to their structures and mechanisms of action. Their proteolytic active sites are usually sequestered in barrel-like structures that prevent uncontrolled proteolysis. These ring shaped proteolytic domains, or proteolytic sub-complexes, are connected to and cooperate with structurally similar ATPase domains or ATPase sub-complexes. Substrates bind to these ATPase domains or ATPase sub-complexes and the energy released by ATP hydrolysis is used to unfold and translocate the substrate into the proteolytic cavity and to activate the proteases themselves. ATP-dependent proteases are present in all prokaryotic and eukaryotic cells. In eukaryotic cells, they are localized in the cytosol and in the nucleus (proteasome) as well as in the organelles: ...
Strikingly, inactivation or loss of the m-AAA protease does not result in the accumulation of long OPA1 isoforms, as predicted by experiments in yeast (Duvezin-Caubet et al., 2007), but decreases their stability. The accelerated cleavage of OPA1 in the absence of the m-AAA protease is mediated by OMA1, a new member of a conserved and widespread family of membrane-bound M48 metallopeptidases. We have previously identified yeast Oma1 in the mitochondrial inner membrane as a peptidase that can substitute for the function of the m-AAA protease during degradation of a misfolded membrane protein (Käser et al., 2003). Similarly, synthetic growth defects have been observed when mutations in the bacterial AAA protease FtsH were combined with mutations in HtpX, which is a distant homologue of OMA1, indicating overlapping proteolytic activities (Shimohata et al., 2002). In agreement with these findings, we demonstrate in this study that mammalian OMA1, similar to the m-AAA protease, can cleave OPA1. The ...
Metalloendopeptidase OMA1, mitochondrial is an enzyme that in humans is encoded by the OMA1 gene. As a metalloprotease, this protein is a substantial component of the quality control system in the inner membrane of mitochondria. Being activated by enzyme Bax and Bak, mitochondrial protease OMA1 promotes cytochrome c release which subsequently induces apoptosis. The gene OMA1 encodes a metalloprotease, a founding member of a conserved family of membrane-embedded metallopeptidases in mitochondria. The human gene has 9 exons and locates at chromosome band 1p32.2-p32.1 The human protein metalloendopetidase OMA1, mitochondrial is 60.1 kDa in size and composed of 524 amino acids with mitochondrial transition peptide (position 1-13). The mature protein has a theoretical pI of 8.44. The inner membrane of mitochondrial houses two AAA proteases and these membrane-embedded peptidases were termed m- and i-AAA proteases to indicate their different topology in the inner membrane. The m-AAA protease is facing ...
FtSH4 showed a high expression level in the rosette leaves, and its transcript levels were stable during different growth stages (Zhang et al., 2014). These results, combined with the premature senescence phenotype of the ftsh4-4 mutant, indicate that FtSH4 may be an upstream regulator of senescence. Although FtSH4 plays important roles in regulating premature senescence by altering the levels of ROS (Gibala et al., 2009; Kicia et al., 2010; Smakowska et al., 2014, 2016), the detailed mechanism behind this process is not clear. ROS are important multifaceted signaling molecules that can regulate a number of cellular pathways and, thus, play critical roles in plant development (Foyer and Noctor, 2013). ROS and autophagy are associated with cell death, and more recent evidence indicates that both ROS and autophagy play important roles in signaling and cellular adaptation to stress (Wang et al., 2011). Mitochondria are known to play key roles in triggering cell death via altering cellular redox to ...
FtsH is an evolutionary conserved membrane-bound metalloprotease complex. While in most prokaryotes FtsH is encoded by a single gene, multiple FtsH genes are found in eukaryotes. Genetic and biochemical data suggest that the Arabidopsis chloroplast FtsH is a hetero-hexamer. This raises the question why photosynthetic organisms require a heteromeric complex, whereas in most bacteria a homomeric one is sufficient. To gain structural information of the possible complexes, the Arabidopsis FtsH2 (type B) and FtsH5 (type A) were modeled. An in silico study with mixed models of FtsH2/5 suggests that heteromeric hexamer structure with ratio of 4∶2 is more likely to exists. Specifically, calculation of the buried surface area at the interfaces between neighboring subunits revealed that a hetero-complex should be thermodynamically more stable than a homo-hexamer, due to the presence of additional hydrophobic and hydrophilic interactions. To biochemically assess this model, we generated Arabidopsis transgenic
The SCOP classification for the FtsH protease domain-like superfamily including the families contained in it. Additional information provided includes InterPro annotation (if available), Functional annotation, and SUPERFAMILY links to genome assignments, alignments, domain combinations, taxonomic visualisation and hidden Markov model information.
Article that discusses some of the complications that emerge when expressing GPCRs in microbial systems. One of the solutions this group found was co-expression of the GPCR-GFP construct with various regulatory proteins involved in membrane metabolism. Coexpression with the AAA+ protease FtsH, an enzyme involvedin MP degradation and quality control. (Article to be read in advance of Mondays meeting ...
cell division protease ftsH homolog 10, mitochondrial, AtFtsH10Anti-FtsH10 | plant fts metallo-protease H10 antibodies, Q8VZI8, Anti-FtsH10 | plant fts metallo-protease H10 antibodies
6NYY: Unique Structural Features of the Mitochondrial AAA+ Protease AFG3L2 Reveal the Molecular Basis for Activity in Health and Disease.
Genetic information processingProtein fateDegradation of proteins, peptides, and glycopeptidesATP-dependent protease HslVU, peptidase subunit (TIGR03692; EC 3.4.25.2; HMM-score: 276.6) ...
The objective of our study was to investigate the effect of Aliskiren, a renin inhibitor, on the deoxycorticosterone (DOCA) induced myocardial fibrosis in a rat model and its underlying mechanism. A total of 45 Sprague-Dawley (SD) rats underwent right nephrectomy and were randomly assigned into 3 groups: control group (CON group: silicone tube was embedded subcutaneously); DOCA treated group (DOC group: 200 mg of DOCA was subcutaneously administered); DOCA and Aliskiren (ALI) treated group (ALI group: 200 mg of DOCA and 50 mg/kg/d ALI were subcutaneously and intragastrically given, respectively). Treatment was done for 4 weeks. Sirius red staining was employed to detect the expression of myocardial collagen, and the myocardial collagen volume fraction (CVF) and perivascular collagen volume area (PVCA) were calculated. Radioimmunoassay was carried out to measure the renin activity (RA) and content of angiotensin II (Ang II) in the plasma and ventricle. Western blot assay was done to detect the ...
ATP-dependent Clp protease proteolytic subunit (ClpP) is an enzyme that in humans is encoded by the CLPP gene. This protein is an essential component to form the protein complex of Clp protease (Endopeptidase Clp). Enzyme ClpP is a highly conserved serine protease present throughout bacterial and also found in the mitochondria and chloroplasts of eukaryotic cells. The ClpP monomer is folded into three subdomains: the handle, the globular head, and the N-terminal region. By itself, ClpP can assemble into a tetradecamer complex (14-members) and form a closed proteolytic chamber. A fully assembled Clp protease complex has a barrel-shaped structure in which two stacked ring of proteolytic subunits (ClpP or ClpQ) are either sandwiched between two rings or single-caped by one ring of ATPase-active chaperon subunits (ClpA, ClpC, ClpE, ClpX or ClpY). ClpXP is presented in almost all bacteria while ClpA is found in the Gram-negative bacteria, ClpC in Gram-Positive bacteria and cyanobacteria. ClpAP, ...
The general pathway involving adenosine triphosphate (ATP)-dependent proteases and ATP-independent peptidases during cytosolic protein degradation is conserved, with differences in the enzymes utilized, in organisms from different kingdoms. Lon and caseinolytic protease (Clp) are key enzymes responsible for the ATP-dependent degradation of cytosolic proteins in Escherichia coli. Orthologs of E. coli Lon and Clp were searched for, followed by multiple sequence alignment of active site residues, in genomes from seventeen organisms, including representatives from eubacteria, archaea, and eukaryotes. Lon orthologs, unlike ClpP and ClpQ, are present in most organisms studied. The roles of these proteases as essential enzymes and in the virulence of some organisms are discussed.
Deg. one of the Escherichia coli systems for degrading abnormal polypeptides (e.g., nonsense fragments), is also involved in the degradation of some classes of missense proteins. Both missense proteins of beta-galactosidase and temperature-sensitive phage products appear to be degraded by the Deg system. Mutations in the Deg system are indistinguishable from mutations classically called lon or capR; all map near proC, all are mucoid, defective in protein degradation, sensitive to radiomimetic agents, and defective in P1 lysogenization. All are able to propagate temperature-sensitive phage better than lon+ parental strains. Mutations that suppress the radiation sensitivity of these strains (sul) also suppress the P1 lysogenization defect, but do not affect mucoidy or the degradation defect.. ...
Immunochemical properties of P-450HFLb purified from human fetal livers were investigated. P-450HFLb cross-reacted with antibodies to rat P-4501A1 but not with antibodies to CYP2A6, CYP2C9, CYP3A7 (P-450HFLa) and rat CYP2B1. In addition, P-450HFLb also cross-reacted with both monospecific antibodies to rat CYP1A1 and CYP1A2. However, P-450HFLb was shown to be an immunochemically distinct form of cytochrome P-450 from P-450PA (human CYP1A2). Immunoblot analysis of human fetal livers with the antibodies to P-450HFLb showed that P-450HFLb was expressed in all fetal livers studied although there appeared to be individual differences in the amounts of P-450HFLb expressed in fetal livers. The formation of mutagens from IQ (but not from AFB1) in fetal liver homogenates was inhibited by the antibodies to P-450HFLb in a dose dependent manner. These results suggest that P-450HFLb may be a form of human cytochrome P-450 classified into CYP1 gene family, and that the cytochrome P-450 is, in part, ...
Lon proteases are distributed in every kingdoms of lifestyle and are necessary for success of cells under tension. absence of bound nucleotide, all six / domains are rotated and out in the way from the L subunits up, which would generate an axial route sufficient to permit unfolded as well as perhaps also small folded XL-888 protein to feed. In every ATP-dependent proteases, substrate gain access to is certainly controlled on the apical surface area of AAA+ domains through axial loops whose positions are transformed in response to rigid area actions as nucleotides bind and so are hydrolysed and released in the AAA+ domains. Multi-component proteases such as for example ClpXP, ClpAP, HslUV (ClpYQ), and 26 S proteasomes, which work as powerful complexes of chaperone and proteolytic elements, control substrate gain access to on the entry towards the protease also. The sequestered proteolytic chambers are built by signing up for two heptamers (or hexamers regarding ClpQ) in person so the energetic ...
Rabbit polyclonal ATP-dependent Clp protease adapter protein ClpS antibody validated for WB, ELISA and tested in E coli. Immunogen corresponding to recombinant…
When nutrients in their environment are exhausted, bacterial cells become arrested for growth. During these periods, a primary challenge is maintaining cellular integrity with a reduced capacity for renewal or repair. Here, we show that the heat-shock protease FtsH is generally required for growth arrest survival of Pseudomonas aeruginosa, and that this requirement is independent of a role in regulating lipopolysaccharide synthesis, as has been suggested for Escherichia coli. We find that ftsH interacts with diverse genes during growth and overlaps functionally with the other heat-shock protease-encoding genes hslVU, lon, and clpXP to promote survival during growth arrest. Systematic deletion of the heat-shock protease-encoding genes reveals that the proteases function hierarchically during growth arrest, with FtsH and ClpXP having primary, nonredundant roles, and HslVU and Lon deploying a secondary response to aging stress. This hierarchy is partially conserved during growth at high temperature ...
Katayama, Y et al. (1988) The two-component, ATP-dependent Clp protease of Escherichia coli. Purification, cloning, and mutational analysis of the ATP-binding component. J. Biol. Chem. 263 15226-36 PubMed GONUTS page ...
SWISS-MODEL Repository entry for A0A1B4HVZ7 (A0A1B4HVZ7_9BURK), ATP-dependent Clp protease adapter protein ClpS. Burkholderia metallica
SWISS-MODEL Repository entry for A0RHK3 (HSLV_BACAH), ATP-dependent protease subunit HslV. Bacillus thuringiensis (strain Al Hakam)
ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.
Turnover of Endogenous SsrA-tagged Proteins Mediated by ATP-dependent Proteases in Escherichia coli*[S with combining enclosing square]: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2516991 ...
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Can anyone help please.. Weve been trying to express a pro-hormone as a GST fusion in E. coli (DH5-alpha) but seem to be having problems with proteolysis - we think this may be occuring at double basic sites but are not completely sure. Has anyone a) had similar problems b) been able to solve the problem by using e.g. JM105s or BL21s c) tried inhibiting endogenous coli proteases (i.e. whilst they are growing) by adding protease inhibitors to the broth (will they get into the cells ?) Thanks in advance Rob Layfield ...
The 26S protease is involved in the ATP-dependent degradation of ubiquitited proteins. The regulatory (or ATPase) complex confers ATP dependency and…
Ramos, M. L. ; Dias, D.C.; Justino, L. L. G. ; Verissimo, L.M.P.; Valente, A. J. M. ; Esteso, M. A. ; Ribeiro, A. C. F. ; Leaist, D.G.; Pina, J. ; Cabral, A.M.T.D.P.V.; Rodrigo, M.M. ...
Stenotrophomonas maltophilia ATP-dependent Clp protease ATP-binding subunit ClpX (clpX) datasheet and description hight quality product and Backed by our Guarantee
Purchase Recombinant Burkholderia cenocepacia ATP-dependent Clp protease adapter protein ClpS(clpS). It is produced in Yeast. High purity. Good price.
p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.,/p> ,p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.,/p> ,p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).,/p> ,p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x,sup>64,/sup> + x,sup>4,/sup> + x,sup>3,/sup> + x + 1. The algorithm is described in the ISO 3309 standard. ,/p> ,p class=publication>Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.,br /> ,strong>Cyclic redundancy and other checksums,/strong>,br /> ,a href=http://www.nrbook.com/b/bookcpdf.php>Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993),/a>),/p> Checksum:i ...
TY - JOUR. T1 - Investigation of the subunit composition and the pharmacology of the mitochondrial ATP-dependent K+ channel in the brain. AU - Lacza, Zsombor. AU - Snipes, James A.. AU - Kis, Béla. AU - Szabó, Csaba. AU - Grover, Gary. AU - Busija, David W.. PY - 2003/12/19. Y1 - 2003/12/19. N2 - Selective activation of mitoKATP channels can protect the brain or cultured neurons against a variety of anoxic or metabolic challenges. However, little is known about the subunit composition or functional regulation of the channel itself. In the present study, we sought to characterize the mitoKATP channel in the mouse brain using overlapping approaches. First, we determined that mitochondria contain the pore-forming Kir6.1 and Kir6.2 subunits with Western blotting, immunogold electron microscopy and the identification of mitochondrial transport sequences. In contrast, we found no evidence for the presence of either known sulfonylurea receptors (SUR1 or SUR2) in the mitochondria. However, the ...
Nicoloff, Hé.; Perreten, V.; McMurry, L.M.; Levy, S.B., 2006: Role for tandem duplication and lon protease in AcrAB-TolC- dependent multiple antibiotic resistance (Mar) in an Escherichia coli mutant without mutations in marRAB or acrRAB
1XHK: The active site of a lon protease from Methanococcus jannaschii distinctly differs from the canonical catalytic Dyad of Lon proteases.
The Cologne Cluster of Excellence in Cellular Stress Responses in Aging-associated Diseases provides an extremely dynamic environment for research into the aging process and its diseases.
Die Universität zu Köln ist eine Exzellenzuniversität mit dem klassischen Fächerspektrum einer Volluniversität. Als eine der größen Hochschulen Europas arbeitet sie in Forschung und Lehre auch international auf höchstem Niveau.
Complete information for YME1L1 gene (Protein Coding), YME1 Like 1 ATPase, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
In mammals, the UPRmt signaling mechanism has been investigated in cell culture models by ethidium bromide treatment (Martinus et al., 1996) and overexpression of aggregation-prone mutant protein ornithine transcarbamylase (OTC) targeted to the mitochondrial matrix (Zhao et al., 2002). Several components of the pathway, such as the mitochondrial chaperones and the quality control protease ClpP were shown to be conserved from C. elegans. However, downstream signaling steps and transcriptional regulation of UPRmt remain not well understood.. In response to unfolded protein stress in mammalian cells, the expression of the nuclear encoded mitochondrial chaperones HSP60, HSP10 and mtDnaJ, and the protease ClpP is induced in a transient manner, the extent of which correlates with the level of unfolded proteins in mitochondria (Zhao et al., 2002). In addition, mitochondrial proteases YME1L1 and PMPCB, the import component TIMM17A and the enzymes NDUFB2, endonuclease G and thioredoxin 2 are all ...
ID CLPP_VESOH Reviewed; 198 AA. AC A5CXJ8; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 12-JUN-2007, sequence version 1. DT 22-NOV-2017, entry version 70. DE RecName: Full=ATP-dependent Clp protease proteolytic subunit {ECO:0000255,HAMAP-Rule:MF_00444}; DE EC=3.4.21.92 {ECO:0000255,HAMAP-Rule:MF_00444}; DE AltName: Full=Endopeptidase Clp {ECO:0000255,HAMAP-Rule:MF_00444}; GN Name=clpP {ECO:0000255,HAMAP-Rule:MF_00444}; GN OrderedLocusNames=COSY_0203; OS Vesicomyosocius okutanii subsp. Calyptogena okutanii (strain HA). OC Bacteria; Proteobacteria; Gammaproteobacteria; OC sulfur-oxidizing symbionts. OX NCBI_TaxID=412965; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HA; RX PubMed=17493812; DOI=10.1016/j.cub.2007.04.039; RA Kuwahara H., Yoshida T., Takaki Y., Shimamura S., Nishi S., Harada M., RA Matsuyama K., Takishita K., Kawato M., Uematsu K., Fujiwara Y., RA Sato T., Kato C., Kitagawa M., Kato I., Maruyama T.; RT Reduced genome of the thioautotrophic ...
After 2 years at MIT as a research associate, she returned to NIH in 1976 to become a senior investigator in the Laboratory of Molecular Biology, continuing studies on these proteases and their substrates. In collaborations with Michael Maurizi in the Laboratory of Cell Biology at NCI, and Sue Wickner in NCIs Laboratory of Molecular Biology, her laboratory has continued to investigate the ATP-dependent proteases of Escherichia coli and their protein targets, studying the mechanism of proteolysis, the basis for target selection and the ways in which unstable proteins are used in regulatory cascades. The architecture and general mechanism of action of the bacterial proteases and their important role in regulating gene expression have proven to be characteristic not only of E. coli, but of eukaryotic organisms as well. This work led to her election to the National Academy of Sciences in 1998 and the American Academy of Arts and Sciences in 1999. Studies on the role of small RNAs in regulation ...
The calcium-signaling network is an important transducer of internal and external stimuli in plants. These signals are transduced by a divers set of calcium-sensors such as calmodulin and calmodulin like proteins. In this work, AFG1L2 (AFG1 like protein 2) was characterized as a calmodulin binding protein that belongs to the family of AAA+ proteins (ATPases associated with various cellular activities). Using GFP fusion constructs it was possible to determine the in vivo localization of AFG1L2 in mitochondria and also to confirm the dual localization of a previously described homologe, AFG1L1, to mitochondria and chloroplasts. The interaction between AFG1L2 and calmodulin is calcium dependent and the calmodulin binding site of the AFG1L2 protein is in the AAA domain at a site homologous to the AFG1L1 protein, in very close proximity to the Walker A Motif, which is essential for ATP hydrolysis. It could be shown that ATP and ADP intensify the interaction between AFG1L2 and calmodulin. AAA-proteins ...
Introduction Mitochondria are essential organelles present in most eukaryotic cells and typically form discrete structures or elaborate tubular networks in the cytoplasm (1). They were first cytologially characterized as bioblasts by Richard Altmann in 1894. Subsequently, they were renamed into mitochondria by Carl Brenda in 1898. Insight into their structure was provided by the first detailed electron microscopy pictures of these organelles in 1952 (2). It has now been well established that mitochondria fulfill a crucial role in a plethora of biological processes (figure 1 adapted from 3). For example, mitochondria are the main source of cellular ATP production, while they also serve as an important cellular storage for calcium, a key signaling molecule. In this way, mitochondria control calcium levels and thereby regulate calcium-dependent signaling pathways. Additionally, mitochondria participate in maintaining redox homeostasis through their production of reactive oxygen species. These drive ...
In the two cases, intracellular S. aureus USA cells showed clear indicators of ongoing cell division Inhibitors Autophagy is regarded an ancient eukaryotic pathway for cellular self digestion that evolved with the endomembrane strategy . Since the endomembrane system offered an opportunity for invading pathogens to manipulate the host cell, its further thought of the autophagic response to pathogen invasion might have also evolved as an early host defense program of eukaryotic cells . Interestingly enough, this hypothesis explains that autophagy is in portion a stochastic degradation pathway to clear the cytoplasm, therefore securing the performance of each proteins plus the endomembrane technique, but can also be a specific response triggered by certain pressure exposures, such as pathogen invasion. In truth, the autophagic response to pathogen invasion is recognized mainly because autophagy related proteins vital to the stochastic practice of autophagy, this kind of as Atg and LC, have also ...
Broadly, I am interested in studying the pathogenic mechanisms of neurodegenerative diseases. I focus on m-AAA protease, which is present in the inner mitochondrial membrane and is involved in protein quality control. In mammals, it exists as a hetero-oligomeric complex composed of two subunits, paraplegin and AFG3L2, and as a homo-oligomeric complex composed of AFG3L2 alone. Mutations in AFG3L2 lead to autosomal dominant spinocerebellar ataxia, SCA 28, while mutations in another subunit, paraplegin, leads to hereditary spastic paraplegia. The m-AAA protease is one of the many instances where there is an intricate connection between mitochondria and neurodegenerative diseases. I attempt to study the mitochondrial dynamics and transport in the neurons of AFG3L2 knock out mouse in vitro to arrive at a plausible explanation for neurodegenerative mechanisms.. ...
Broadly, I am interested in studying the pathogenic mechanisms of neurodegenerative diseases. I focus on m-AAA protease, which is present in the inner mitochondrial membrane and is involved in protein quality control. In mammals, it exists as a hetero-oligomeric complex composed of two subunits, paraplegin and AFG3L2, and as a homo-oligomeric complex composed of AFG3L2 alone. Mutations in AFG3L2 lead to autosomal dominant spinocerebellar ataxia, SCA 28, while mutations in another subunit, paraplegin, leads to hereditary spastic paraplegia. The m-AAA protease is one of the many instances where there is an intricate connection between mitochondria and neurodegenerative diseases. I attempt to study the mitochondrial dynamics and transport in the neurons of AFG3L2 knock out mouse in vitro to arrive at a plausible explanation for neurodegenerative mechanisms.. ...
We report the identification of disruptions in 19 genes and one intergenic mutation that negatively affect biofilm formation in S. aureus. With the exception of multiple insertions in each gene of the icaADBC operon, we uncovered none of the genes previously described for their role in biofilm formation in staphylococci. For example, we did not identify Em-Mu insertions in genes encoding subunits of the Clp ATP-dependent proteases, rbf, sarA, dtlA, atlE, hla, and rsbU. Our screen was large but not saturating, and other biofilm-defective mutants await identification. We do not report a screen for increased biofilm formation with S30. Interestingly, a recent study describes such an increased biofilm screen in another S. aureus human clinical isolate and points to the discovery of an ica-independent biofilm pathway active in the absence of the ArlRS two-component sensor (67).. Three mutations were functionally complemented for their biofilm defect by reintroducing cloned genes coding for MgrA, ...
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Alternatively, YME1L degradation could decrease the capacity for cells to regulate inner membrane proteostasis. To explore this potential consequence of YME1L degradation, we monitored the impact of oxidative stress on YME1L‐mediated regulation of the TIM23 mitochondrial protein import complex [30]. Mammalian TIM23 forms two exclusive complexes containing distinct core interactions between the subunit Tim23 and one of the two mammalian paralogs of yeast Tim17, Tim17A, or Tim17B [31]. Previous work showed that Tim17A is a stress‐regulated TIM23 subunit that is rapidly degraded by YME1L in response to eIF2α phosphorylation‐dependent translational attenuation [30]. However, Tim17B is not subject to this regulation. Thus, YME1L‐mediated degradation of Tim17A reduces the population of active TIM23 complexes containing a core Tim23-Tim17A interaction without impacting TIM23 complexes containing a core Tim23-Tim17B interaction [30]. This provides a mechanism for cells to sensitively attenuate, ...
Alternatively, YME1L degradation could decrease the capacity for cells to regulate inner membrane proteostasis. To explore this potential consequence of YME1L degradation, we monitored the impact of oxidative stress on YME1L‐mediated regulation of the TIM23 mitochondrial protein import complex [30]. Mammalian TIM23 forms two exclusive complexes containing distinct core interactions between the subunit Tim23 and one of the two mammalian paralogs of yeast Tim17, Tim17A, or Tim17B [31]. Previous work showed that Tim17A is a stress‐regulated TIM23 subunit that is rapidly degraded by YME1L in response to eIF2α phosphorylation‐dependent translational attenuation [30]. However, Tim17B is not subject to this regulation. Thus, YME1L‐mediated degradation of Tim17A reduces the population of active TIM23 complexes containing a core Tim23-Tim17A interaction without impacting TIM23 complexes containing a core Tim23-Tim17B interaction [30]. This provides a mechanism for cells to sensitively attenuate, ...
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Hershko, A., Ciechanover, A., Heller, H., Haas, A.L., and Rose I.A. (1980) „Proposed role of ATP in protein breakdown: Conjugation of proteins with multiple chains of the polypeptide of ATP-dependent proteolysis. Proc. Natl. Acad. Sci. USA 77, pp. 1783-1786 ...
1OFH: Structure and Reactivity of an Asymmetric Complex between Hslv and I-Domain Deleted Hslu, a Prokaryotic Homolog of the Eukaryotic Proteasome
Visit Healthgrades for information on Dr. Lon Raby Jr, MD Find Phone & Address information, medical practice history, affiliated hospitals and more.
2014, Roohit Inc. Hilight™ Protected by patents numbered 7,844,891, 7,966,623, 8,156,178, 8,352,573 and 8,661,031. Additional patents pending. ...
Dr. Michael Eblan, MD is a Radiation Oncology Specialist in Fairfax, VA. He is affiliated with medical facilities such as Inova Alexandria Hospital and Inova Fair Oaks Hospital. He is accepting new patients. Be sure to call ahead with Dr. Eblan to book an appointment.
Partial substrate degradation by ATP-dependent proteases". IUBMB Life. 66 (5): 309-317. doi:10.1002/iub.1271. PMID 24823973. ... Later, the ATP-dependent proteolytic complex that was responsible for ubiquitin-dependent protein degradation was discovered ... After a protein has been ubiquitinated, it is recognized by the 19S regulatory particle in an ATP-dependent binding step. The ... Ciehanover A, Hod Y, Hershko A (April 1978). "A heat-stable polypeptide component of an ATP-dependent proteolytic system from ...
Lon protease is a member of ATP-dependent proteases (AAA+ proteases). Mature and catalytically viable human lon protease ... "A human mitochondrial ATP-dependent protease that is highly homologous to bacterial Lon protease". Proceedings of the National ... Lu B, Liu T, Crosby JA, Thomas-Wohlever J, Lee I, Suzuki CK (March 2003). "The ATP-dependent Lon protease of Mus musculus is a ... Lu B, Liu T, Crosby JA, Thomas-Wohlever J, Lee I, Suzuki CK (March 2003). "The ATP-dependent Lon protease of Mus musculus is a ...
Van Dyck L, Langer T (November 1999). "ATP-dependent proteases controlling mitochondrial function in the yeast Saccharomyces ... ATP-dependent metalloprotease YME1L1 is an enzyme that in humans is encoded by the YME1L1 gene. YME1L1 belongs to the AAA ... an ATP/GTP binding motif, and a HEXXH motif typical of a zinc-dependent binding domain. YME1L1 is embedded in the inner ... Anand R, Wai T, Baker MJ, Kladt N, Schauss AC, Rugarli E, Langer T (March 2014). "The i-AAA protease YME1L and OMA1 cleave OPA1 ...
... (EC 3.4.21.92, endopeptidase Ti, caseinolytic protease, protease Ti, ATP-dependent Clp protease, ClpP, Clp ... Endopeptidase CLP protease family ATP-dependent Clp protease proteolytic subunit Gottesman S, Clark WP, Maurizi MR (May 1990 ... Maurizi MR, Thompson MW, Singh SK, Kim SH (1994). "Endopeptidase Clp: ATP-dependent Clp protease from Escherichia coli". ... "The ATP-dependent Clp protease of Escherichia coli. Sequence of clpA and identification of a Clp-specific substrate". The ...
ATP-dependent serine proteinase, lon proteinase, protease La, proteinase La, ATP-dependent lon proteinase, ATP-dependent ... A heat-shock gene which encodes the ATP-dependent protease La". The Journal of Biological Chemistry. 263 (24): 11718-28. PMID ... Larimore FS, Waxman L, Goldberg AL (April 1982). "Studies of the ATP-dependent proteolytic enzyme, protease La, from ... gene lon protease, gene lon proteins, PIM1 protease, PIM1 proteinase, serine protease La) is an enzyme. This enzyme catalyses ...
The ATP-dependent proteases are shown to maintain the level of regulatory proteins and to get rid of any misfolded or damaged ... Along with the ATP-dependent proteases, the small RNA molecules are an important part of this response. For example, one of ... Susan Gottesman is known for her work with small RNAs and ATP-dependent proteases. Her work in these subjects has been ... In Gottesman's studies, she showed that the ATP-dependent proteases are regulated by the delivery of their substrate molecules ...
The polyubiquinated protein is targeted to an ATP-dependent protease complex, the proteasome. The ubiquitin is released and ... Cysteine protease Serine protease Threonine protease Aspartic protease Glutamic protease Metalloprotease Asparagine peptide ... Proteases may be regulated by antiproteases or protease inhibitors, and imbalance between proteases and antiproteases can ... The proteases used have high degree of specificity, such as thrombin, enterokinase, and TEV protease, so that only the targeted ...
Encoding a Mitochondrial ATP-Dependent Chambered Protease". The American Journal of Human Genetics. 92 (4): 605-613. doi: ...
The protein encoded by this gene is an ATP-dependent protease that likely plays a role in maintaining overall peroxisome ... "Cleavage site selection within a folded substrate by the ATP-dependent lon protease". J. Biol. Chem. 280 (26): 25103-10. doi: ...
Higgins JJ, Pucilowska J, Lombardi RQ, Rooney JP (November 2004). "A mutation in a novel ATP-dependent Lon protease gene in a ...
This large family of proteins mediate docking of synaptic vesicles in an ATP-dependent manner. With the help of synaptobrevin ... The botulinum toxin has protease activity which degrades the SNAP-25 protein. The SNAP-25 protein is required for vesicle ... The ability of SNAREs to mediate fusion in a calcium-dependent manner recently has been reconstituted in vitro. Consistent with ... The release is regulated by a voltage-dependent calcium channel. Vesicles are essential for propagating nerve impulses between ...
It uses the helicase ATP hydrolysis site to remove the γ-phosphate from the 5′ end of the RNA. The N-terminal domain of the non ... One of the products cleaved is a RNA-dependent RNA polymerase, responsible for the synthesis of a negative-sense RNA molecule. ... Once translated, the polyprotein is cleaved by a combination of viral and host proteases to release mature polypeptide products ... RNA binding affinity is reduced by the presence of ATP or GTP and enhanced by S-adenosyl methionine. This protein also encodes ...
PreP is an Zn2+-dependent and ATP-independent metalloprotease, it doesn't select substrates on the basis of post-translational ... Sauer RT, Baker TA (2011). "AAA+ proteases: ATP-fueled machines of protein destruction". Annual Review of Biochemistry. 80: 587 ... PreP is the Aβ-degrading protease in mitochondria. Immune-depletion of PreP in brain mitochondria prevents degradation of ... Chen J, Teixeira PF, Glaser E, Levine RL (December 2014). "Mechanism of oxidative inactivation of human presequence protease by ...
The RadA/Sms family are probable ATP-dependent proteases involved in both DNA repair and degradation of proteins, peptides, ... It binds ATP. Also in the KaiC family is RadA/Sms, a highly conserved eubacterial protein that shares sequence similarity with ... They did this by adding KaiA, KaiB, KaiC, and ATP into a test tube in the approximate ratio recorded in vivo. They then ... In both systems the circadian period is dependent on the interactions between proteins within the cell, and when the genes for ...
Clp-family proteins are ATP-dependent proteases which play a crucial role in the cell function by degrading misfolded proteins ... activation of casein lytic protease (ClpP) which is an important bacterial protease. Most antibiotics work through inhibitory ... They bind to ClpP and allow the protease to degrade proteins without the help of an ATPase. ADEP4/ClpP complexes target ... This process is tightly regulated with the hydrolysis of ATP to prevent uncontrolled protein or peptide degradation that would ...
Kanemori M, Nishihara K, Yanagi H, Yura T (December 1997). "Synergistic roles of HslVU and other ATP-dependent proteases in ... 1996). HslV-HslU: A novel ATP-dependent protease complex in Escherichia coli related to the eukaryotic proteasome. Proc Natl ... by the ATP-dependent HslVU protease from Escherichia coli". FEBS Letters. 553 (3): 351-4. doi:10.1016/s0014-5793(03)01044-5. ... "Purification and characterization of the heat shock proteins HslV and HslU that form a new ATP-dependent protease in ...
... the ATP-dependent substrate specificity component of the ClpP-ClpX protease, is a novel molecular chaperone". The EMBO Journal ... Blond-Elguindi S, Fourie AM, Sambrook JF, Gething MJ (June 1993). "Peptide-dependent stimulation of the ATPase activity of the ... Non-chaperonin molecular chaperone ATPase (EC 3.6.4.10, molecular chaperone Hsc70 ATPase) is an enzyme with systematic name ATP ... "Unfolded proteins stimulate molecular chaperone Hsc70 ATPase by accelerating ADP/ATP exchange". Biochemistry. 31 (39): 9406-12 ...
The predicted structure is Chain A, crystal structure analysis of Clpb, a protein that encodes an ATP-dependent protease and ...
This rapid synthesis indicates that there is an ATP-dependent interaction where the formed HSP60 complex stabilizes the ... The subsequent protease-resistant HSP60 is formed in a half-time of 5-10 minutes. ... The addition of ATP and GroES has a drastic effect on the conformation of the cis domain. This effect is caused by flexion and ... Hydrolysis of ATP and binding of a new substrate protein to the opposite cavity sends an allosteric signal causing GroES and ...
ATP-dependent Clp protease ATP-binding subunit clpX-like, mitochondrial is an enzyme that in humans is encoded by the CLPX gene ... ATP binding can stabilize the association between ClpX and ClpP ring structures. In Mycobacteria, the ClpXP protease is ... ClpP2 ClpX is an ATP-dependent chaperone that can recognize protein substrates by binding to protein degradation tags. These ... During protease Clp complex assembly, the ClpX subunits form a hexameric ring structure. According to the orientation of ClpX ...
Similarly, because host Hfl-proteases degrade proteins in an ATP dependent manner, coupling cII levels to Hfl-protease activity ... Host protease dependent degradation: C-terminal degradation tag is recognized by host HflA and HflB proteases, quickly ... This tag is recognized by host proteases HflA and HflB, cause rapid proteolysis cII. Although the C-terminal tag is still ... Krinke L, Wulff DL (December 1990). "RNase III-dependent hydrolysis of lambda cII-O gene mRNA mediated by lambda OOP antisense ...
ClpS is as a specific adaptor protein for the ATP-dependent AAA+ protease ClpAP, and hence ClpS delivers N-degron substrates to ... it involves the Clp protease system which consists of the adaptor protein ClpS and the ClpA/P chaperone and protease core. A ... June 2013). "ClpS1 is a conserved substrate selector for the chloroplast Clp protease system in Arabidopsis". The Plant Cell. ... Nishimura K, van Wijk KJ (September 2015). "Organization, function and substrates of the essential Clp protease system in ...
... triggering the ATP-dependent unfolding of the target protein that allows passage into the proteasome's 20S core particle, where ... proteases degrade the target into short peptide fragments for recycling by the cell. A ubiquitin-activating enzyme, or E1, ...
... atp-dependent proteases MeSH D08.811.277.656.149.200 - endopeptidase clp MeSH D08.811.277.656.149.500 - protease la MeSH ... cyclin-dependent kinase 5 MeSH D08.811.913.696.620.682.700.200.067.900 - cyclin-dependent kinase 9 MeSH D08.811.913.696.620.682 ... cyclin-dependent kinase 4 MeSH D08.811.913.696.620.682.700.200.515 - cyclin-dependent kinase 6 MeSH D08.811.913.696.620.682. ... cyclin-dependent kinase 5 MeSH D08.811.913.696.620.682.700.646.500.750 - cyclin-dependent kinase 2 MeSH D08.811.913.696.620.682 ...
... may refer to: CLP protease family, a family of proteolytic enzymes Endopeptidase Clp, an enzyme complex ATP-dependent Clp ... protease proteolytic subunit, a catalytic subunit of the Clp complex (encoded by the CLPP gene in humans) Local Public Planning ...
... or no longer required for cellular function can also be ubiquitin tagged for degradation by ATP dependent proteases, such as ...
Degradation occurs via ClpXP, a barrel-shaped protease composed of two six-subunit rings of the ATP-dependent ClpX chaperone ... Additional RpoS-dependent factors that determine the size and shape of the cell include the morphogene bolA and products of the ... Discovery of RpoS-dependent virulence genes in Salmonella is consistent with RpoS as a general regulator of the stress response ... RpoS-dependent genes involved in changes in cell membrane permeability and general cell morphology mostly belong to the osm ...
... kills Mycobacterium tuberculosis by targeting the ATP-dependent protease ClpC1P1P2. Chem Biol 21: 509-518. PMCID: PMC4060151 ... by activating the C1 ATPase subunit of the ClpC1P1P2 protease, causing ATP depletion and death. In early 2000s, Lewis began ... His research further showed that persisters are cells with low level of ATP, which drops as a result of stochastic variation in ... He discovered that acyldepsipeptide (ADEP) kills persisters in S. aureus and other bacteria by activating the Clp protease, ...
These subunits can be categorized into two classes based on the ATP dependence of subunits, ATP-dependent subunits and ATP- ... 26S protease regulatory subunit 6B, also known as 26S proteasome AAA-ATPase subunit Rpt3,is an enzyme that in humans is encoded ... Dubiel W, Ferrell K, Rechsteiner M (1994). "Tat-binding protein 7 is a subunit of the 26S protease". Biol. Chem. Hoppe-Seyler. ... The human protein 26S protease regulatory subunit 6B is 47kDa in size and composed of 418 amino acids. The calculated ...
These subunits can be categorized into two classes based on the ATP dependence of subunits, ATP-dependent subunits and ATP- ... 26S protease regulatory subunit 4, also known as 26S proteasome AAA-ATPase subunit Rpt2, is an enzyme that in humans is encoded ... Dubiel W, Ferrell K, Pratt G, Rechsteiner M (1992). "Subunit 4 of the 26 S protease is a member of a novel eukaryotic ATPase ... In humans the 26S protease regulatory subunit 4', also known as 26S proteasome AAA-ATPase subunit Rpt2, is an enzyme that is ...
atp-dependent protease. ribosomal proteins. tRNAs. nicotiana tabacum. edit · image. Chloroplast DNA Interactive gene map of ... After a chloroplast polypeptide is synthesized on a ribosome in the cytosol, ATP energy can be used to phosphorylate, or add a ... A protein kinase drifting around on the outer chloroplast membrane can use ATP to add a phosphate group to the Toc34 protein, ... an energy molecule similar to ATP attaches to Toc34, the protein becomes much more able to bind to many chloroplast preproteins ...
Gottesman MM, Fojo T, Bates SE (January 2002). "Multidrug resistance in cancer: role of ATP-dependent transporters". Nat. Rev. ... "A presenilin-1-dependent gamma-secretase-like protease mediates release of Notch intracellular domain". Nature. 398 (6727): 518 ... Notch receptor processing, ligand-dependent. • positive regulation of phosphorylation. • astrocyte activation. • synapse ... positive regulation of proteasomal ubiquitin-dependent protein catabolic process. • L-glutamate transport. • brain ...
Partial substrate degradation by ATP-dependent proteases". IUBMB Life. 66 (5): 309-317. doi:10.1002/iub.1271. PMID 24823973.. ... the ATP-dependent proteolytic complex that was responsible for ubiquitin-dependent protein degradation was discovered and was ... After a protein has been ubiquitinated, it is recognized by the 19S regulatory particle in an ATP-dependent binding step.[15][ ... Ciehanover A, Hod Y, Hershko A (April 1978). "A heat-stable polypeptide component of an ATP-dependent proteolytic system from ...
ATP-dependent protein binding. • metal ion binding. • tubulin binding. • protein binding. • identical protein binding. • copper ... The protein can exist in multiple isoforms, the normal PrPC and protease-resistant forms designated PrPRes such as the disease- ... protease binding. • glycosaminoglycan binding. • type 5 metabotropic glutamate receptor binding. • type 8 metabotropic ... The ability to bind copper is, therefore, pH-dependent. NMR shows copper binding results in a conformational change at the N- ...
In later research, the oriented peptide library approach has also been used to characterize protease cleavage specificity.[32] ... Auger KR, Serunian LA, Soltoff SP, Libby P, Cantley LC (April 1989). "PDGF-dependent tyrosine phosphorylation stimulates ... where he discovered that an impurity in commercial preparations of ATP, vanadate, acts as a transition state analog for ... Turk BE, Huang LL, Piro ET, Cantley LC (July 2001). "Determination of protease cleavage site motifs using mixture-based ...
ATP-dependent association of the nucleotide binding cassettes during the catalytic cycle of ATP-binding cassette transporters ... Spectroscopic, protease accessibility and crosslinking studies have shown that ATP binding to the NBDs induces conformational ... Substrates of the transporter are taken up into the vesicles in an ATP dependent manner. Rapid filtration using glass fiber ... In these transporters, ATP is bound to the ABC domain. Two molecules of ATP are positioned at the interface of the dimer, ...
Caspases are proteins that are highly conserved, cysteine-dependent aspartate-specific proteases. There are two types of ... Once cytochrome c is released it binds with Apoptotic protease activating factor - 1 (Apaf-1) and ATP, which then bind to pro- ... In order to be released, the protein is cleaved by a calcium-dependent calpain protease. ... IAP also normally suppresses the activity of a group of cysteine proteases called caspases,[33] which carry out the degradation ...
A prominent kinase is cyclin-dependent kinase (or CDK), which comprises a sub-family of protein kinases. As their name implies ... The reaction catalyzed by CDK is as follows: ATP + a target protein → {\displaystyle \rightarrow } ADP + a phosphoprotein. ... protease, and acid/base phosphatase. Prior to the realization that individual enzymes were capable of such a task, it was ... Yee A, Wu L, Liu L, Kobayashi R, Xiong Y, Hall FL (Jan 1996). "Biochemical characterization of the human cyclin-dependent ...
... interacts with filamentous actin to generate force through magnesium-dependent hydrolysis of ATP. The neck acts as a lever arm ... "Cleavage of human and mouse cytoskeletal and sarcomeric proteins by human immunodeficiency virus type 1 protease. Actin, ... ATP binding. • RNA binding. • cadherin binding. • actin filament binding. • microtubule motor activity. • microtubule binding. ... actin-dependent ATPase activity. • calmodulin binding. • ATPase activity. • protein domain specific binding. • actin binding. • ...
ATP-dependent Clp protease proteolytic subunit. B. *Batroxobin. *Brachyurin. C. *C-terminal processing peptidase ...
Phosphorylation by cAMP-dependent protein kinasesEdit. Cyclic AMP-dependent protein kinases (protein kinase A) are activated by ... Adenylyl cyclase is a 12-transmembrane glycoprotein that catalyzes ATP to form cAMP with the help of cofactor Mg2+ or Mn2+. The ... However, protease-activated receptors are activated by cleavage of part of their extracellular domain.[44] ... G-protein-dependent signalingEdit. There are three main G-protein-mediated signaling pathways, mediated by four sub-classes of ...
More formally, it is an ATP-dependent efflux pump with broad substrate specificity. It exists in animals, fungi, and bacteria, ... HIV-type 1 antiretroviral therapy agents like protease inhibitors and nonnucleoside reverse transcriptase inhibitors. ... P-gp is an ATP-dependent drug efflux pump for xenobiotic compounds with broad substrate specificity. It is responsible for ... ATP binds at the cytoplasmic side of the protein. Following binding of each, ATP hydrolysis shifts the substrate into a ...
2.5 ATP per NADH and ~1.5 ATP per UQH2, further reducing the total net production of ATP to approximately 30.[19] An assessment ... The conversion of D-threo-isocitrate to 2-oxoglutarate is catalyzed in eukaryotes by the NAD+-dependent EC 1.1.1.41, while ... In protein catabolism, proteins are broken down by proteases into their constituent amino acids. Their carbon skeletons (i.e. ... or ADP→ATP instead of GDP→GTP,[15] generates 1 ATP or equivalent.. Condensation reaction of GDP + Pi and hydrolysis of succinyl ...
Despite being lipophilic, T3 and T4 cross the cell membrane via carrier-mediated transport, which is ATP-dependent.[34] ... Proteolysis by various proteases liberates thyroxine and triiodothyronine molecules - Efflux of thyroxine and triiodothyronine ... However, at least 10 different active, energy-dependent and genetically-regulated iodothyronine transporters have been ... of the modified protein by proteases then liberates T3 and T4, as well as the non-coupled tyrosine derivatives MIT and DIT.[ ...
In an ATP dependent enzymatically catalyzed reaction, acetyl-CoA is carboxylated to form malonyl-CoA. Acetyl-CoA and malonyl- ... proteases, alcohol dehydrogenase, and esterases. Archaea represent a source of novel chemical compounds also, for example ...
Phagocytes further release proteases that break down the ECM of neighbouring tissue, freeing the activated fibroblasts to ... Glucose is the most prominent source of fuel and it is used to create cellular ATP, providing energy for angiogenesis and the ... Successful wound healing is dependent on various cell types, molecular mediators and structural elements.[96] ... Cells can only migrate over living tissue,[42] so they must excrete collagenases and proteases like matrix metalloproteinases ( ...
Cyclohexanedione targets the Acetyl-CoA carboxylase which is involved in the first step of fat synthesis: ATP-dependent ... HIV protease inhibitors are used to treat patients having AIDS virus by preventing its DNA replication. HIV protease is used by ... HIV protease belongs to aspartic protease family and has a similar mechanism. Firstly the aspartate residue activates a water ... Many enzymes including serine protease, cysteine protease, protein kinase and phosphatase evolved to form transient covalent ...
The BCR-ABL tyrosine kinase activates Ras via phosphorylation of the GAB2 protein, which is dependent on BCR-located ... when bound to ATP and triggers downstream pathways. The ABL tyrosine kinase activity of BCR-Abl is elevated relative to wild- ... have also been identified in downregulating BCR-ABL kinase translation and promoting its degradation by protease.[23][24] ... BCR-ABL fusion cells also exhibit constitutively high levels of activated Ras bound to GTP, activating a Ras-dependent ...
কলি বেক্টেৰিয়াৰ পৰা আহৰণ কৰা DNA লাইগেজ এনজাইমৰ সক্ৰিয়কৰণৰ বাবে ATP অণু আৰু NAD+ প্ৰয়োজন হয় আকৌ লেম্ব্‌ডা T4 ফাজৰ DNA ... Protease) উৎসেচকৰ সহায়ত অধক্ষেপিত কৰি ঘূৰ্ণন প্ৰক্ৰিয়াৰে পৃথক কৰা হয়। (vi) RNAখিনি আতৰ কৰিবলৈ ৰিব'নিউক্লিয়েজ (Ribonuclease ... ইয়াৰ আন এটা নাম হ'ল RNA dependant DNA synthetase। ইয়াক ৰিট্ৰোভাইৰাছৰ (Eg- Rous Sarcoma virus/ RSV, Mouse Mammary tumour virus ... পলিনিউক্লিয়'টাইড কাইনেজে ATP অণুৰ পৰা এটা ফছফেট DNA নাইবা RNA ৰ 5´-OH ফছফেটৰহিত (Dephosphorylated) ...
This is a protease which cleaves a cellular kinase called PBS1. The modified kinase is sensed by RPS5 NLR.[16] ... Under normal conditions, there is a lot more ATP present in the cytoplasm than ADP, and this arrangement of the NLR proteins ... It has also been shown that HR is dependent on the light conditions, which could be linked to the activity of chloroplasts and ... Only when a virulence factor is sensed, the ADP is exchanged for ATP.[14] ...
Protease inhibitors and statins taken together may increase the blood levels of statins and increase the risk for muscle injury ... Ferdinand KC (February 2011). "Are cardiovascular benefits in statin lipid effects dependent on baseline lipid levels?". ... HIV-positive people taking protease inhibitors Atorvastatin, pravastatin or fluvastatin Negative interactions are more likely ... The FDA notified healthcare professionals of updates to the prescribing information concerning interactions between protease ...
קשירת ATP. • transcription factor binding. • קשירת יוני מתכת. • protein phosphatase 2A binding. • enzyme binding. • RNA ... protease binding. • damaged DNA binding. • GO:0001948 קשירת חלבונים. • histone acetyltransferase binding. • copper ion binding ... proteasome-mediated ubiquitin-dependent protein catabolic process. • regulation of signal transduction by p53 class mediator. • ...
response to ATP. • negative regulation of phagocytosis. • response to organic cyclic compound. • protein kinase B signaling. • ... ubiquitin-specific protease binding. • ionotropic glutamate receptor binding. • protein tyrosine kinase binding. • inositol-1,3 ... regulation of cyclin-dependent protein serine/threonine kinase activity. • regulation of cellular component size. • response to ... negative regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S transition of mitotic cell ...
There are sex-dependent differences in regional fat distribution. In women, estrogen is believed to cause fat to be stored in ... often protease inhibitors, a group of medications against AIDS). Central obesity is a symptom of Cushing's syndrome[13] and is ... ATP III Final Report). National Institutes of Health. p. II-17.. ... ATP III Final Report). National Institutes of Health. p. II-27. ...
When ATP levels rise, ATP binds an allosteric site in PFK1 to decrease the rate of the enzyme reaction; glycolysis is inhibited ... Many of these are activated by the trypsin protease, so it is important to inhibit the activity of trypsin in the pancreas to ... Under these conditions, traditional Michaelis-Menten kinetics give a false value for Ki, which is time-dependent. The true ... This catabolic pathway consumes glucose and produces ATP, NADH and pyruvate. A key step for the regulation of glycolysis is an ...
CFTR channels rely on ATP for two main purposes. Firstly, the binding and hydrolysis of ATP has to occur at two nucleotide ... Pyocyanin contributes to the disproportion of protease and antiprotease activity by disabling α1- protease inhibitor. ... ABC transporters called pgp-1 and pgp-2 which are effectively able to extrude intracellular pyocyanin in an energy dependent ... PKA II is activated by cAMP which is produced from ATP. Both these processes are impaired when ATP is depleted by pyocyanin. ...
A diferenza da ATP sintase de tipo F, a ATPase de tipo V ten moitas subunidades relacionadas no anel c; en fungos como os ... Esta acidificación activa as proteases necesarias para a perforación da membrana do ovo durante a fecundación. As ATPases V da ... September 2004). "TCIRG1-dependent recessive osteopetrosis: mutation analysis, functional identification of the splicing ... A hidrólise do ATP nos sitios de unión do nucleótido catalítico na subunidade A impulsa a rotación dun talo central composto ...
2bzz: CRYSTAL STRUCTURES OF EOSINOPHIL-DERIVED NEUROTOXIN IN COMPLEX WITH THE INHIBITORS 5'-ATP, AP3A, AP4A AND AP5A ... 2c01: CRYSTAL STRUCTURES OF EOSINOPHIL-DERIVED NEUROTOXIN IN COMPLEX WITH THE INHIBITORS 5'-ATP, AP3A, AP4A AND AP5A ... 2c02: CRYSTAL STRUCTURES OF EOSINOPHIL-DERIVED NEUROTOXIN IN COMPLEX WITH THE INHIBITORS 5'-ATP, AP3A, AP4A AND AP5A ... 2c05: CRYSTAL STRUCTURES OF EOSINOPHIL-DERIVED NEUROTOXIN IN COMPLEX WITH THE INHIBITORS 5'-ATP, AP3A, AP4A AND AP5A ...
It acts through ATP-dependent conformational changes that on occasion require several rounds of liberation and catalysis in ... During programmed cell death the ICE/ced-3 family of proteases (one of the interleukin-1β-converter proteases) degrade actin ... Role of ATP hydrolysis. As indicated above, although actin hydrolyzes ATP, everything points to the fact that ATP is not ... Higher concentration of ATP in the nucleus (compared to the cytoplasm) promote ADP to ATP exchange in the actin-cofilin complex ...
... the ATP-dependent Clp protease adaptor protein ClpS is a bacterial protein. In the bacterial cytosol, ATP-dependent protein ... Endopeptidase Clp Clp protease family Varshavsky A (August 2011). "The N-end rule pathway and regulation by proteolysis". ... The protein substrate is then degraded by the ClpAP protease. In molecular biology, ... degradation is performed by several different chaperone-protease pairs, including ClpAP. ClpS directly influences the ClpAP ...
ATP-dependent Clp protease proteolytic subunit (ClpP) is an enzyme that in humans is encoded by the CLPP gene. This protein is ... 2002). "Functional proteolytic complexes of the human mitochondrial ATP-dependent protease, hClpXP". J. Biol. Chem. 277 (23): ... ATP-dependent protease from Escherichia coli". The Journal of Biological Chemistry. 262 (10): 4477-85. PMID 3549708. Corydon, ... "Entrez Gene: CLPP ClpP caseinolytic peptidase, ATP-dependent, proteolytic subunit homolog (E. coli)". Katayama-Fujimura, Y; ...
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
MULTISPECIES: ATP-dependent Clp protease adapter ClpS [Leptospira] MULTISPECIES: ATP-dependent Clp protease adapter ClpS [ ... MULTISPECIES: ATP-dependent Clp protease adapter ClpS [Leptospira]. NCBI Reference Sequence: WP_004460163.1 ...
New insights into the ATP-dependent Clp protease: Escherichia coli and beyond.. Porankiewicz J1, Wang J, Clarke AK. ... Much of this directed protein turnover is performed by proteases that require ATP and, of those in bacteria, the Clp protease ...
Rabbit polyclonal ATP-dependent Clp protease adapter protein ClpS antibody validated for WB, ELISA and tested in E coli. ... Anti-ATP-dependent Clp protease adapter protein ClpS antibody. See all ATP-dependent Clp protease adapter protein ClpS primary ... Anti-ATP-dependent Clp protease adapter protein ClpS antibody (ab193643) at 2 µg/ml + DH5a lysate. Secondary. Goat polyclonal ... Western blot - Anti-ATP-dependent Clp protease adapter protein ClpS antibody (ab193643) ...
Molecular model of the bacterial enzyme HsIUV protease. Proteases are enzymes that break down proteins. HsIUV is expressed in ... Caption: ATP-dependent protease. Molecular model of the bacterial enzyme HsIUV protease. Proteases are enzymes that break down ... Keywords: artwork, atp-dependent protease, bacterial, biochemical, biochemistry, biological, biology, cut out, cut outs, cut- ...
ATP-dependent Clp protease proteolytic subunit. A, B, C, D, E, F, G, H, I, J, K, L, M, N. 195. Coxiella burnetii RSA 331. ... Structure of the ClpP subunit of the ATP-dependent Clp Protease from Coxiella burnetii. Anderson, S.M., Wawrzak, Z., Gordon, E. ... Structure of the ClpP subunit of the ATP-dependent Clp Protease from Coxiella burnetii. *DOI: 10.2210/pdb3Q7H/pdb ...
May play the role of a master protease which is attracted to different substrates by different specificity factors such as ClpA ... Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major ... ATP-dependent Clp protease proteolytic subunitAdd BLAST. 193. Keywords - PTMi. Zymogen. Proteomic databases. jPOST - Japan ... ATP-dependent Clp protease proteolytic subunitUniRule annotation. Manual assertion according to rulesi ...
Protease component of the Clp complex that cleaves peptides and various proteins in an ATP-dependent process. Has low peptidase ... ATP-dependent Clp protease proteolytic subunit, mitochondrial. ,p>This subsection of the PTM / Processing section describes ... Protease component of the Clp complex that cleaves peptides and various proteins in an ATP-dependent process. Has low peptidase ... ATP-dependent Clp protease proteolytic subunit, mitochondrial (EC:3.4.21.92). Alternative name(s): ...
... dependent proteases and ATP-independent peptidases during cytosolic protein degradation is conserved, with differences in the ... Lon and caseinolytic protease (Clp) are key enzymes respons … ... genomics and functional roles of the ATP-dependent proteases ... The general pathway involving adenosine triphosphate (ATP)-dependent proteases and ATP-independent peptidases during cytosolic ... Lon and caseinolytic protease (Clp) are key enzymes responsible for the ATP-dependent degradation of cytosolic proteins in ...
Thus, a set of ATP-dependent proteases appear to play synergistic roles in the negative control of the heat shock response by ... We report here that a multicopy plasmid carrying the hslVU operon encoding a novel ATP-dependent protease inhibits the heat ... Synergistic roles of HslVU and other ATP-dependent proteases in controlling in vivo turnover of sigma32 and abnormal proteins ... Synergistic roles of HslVU and other ATP-dependent proteases in controlling in vivo turnover of sigma32 and abnormal proteins ...
... Halperin, Tami ... Using β-casein as a substrate, plant mitochondria possessed an ATP-stimulated, serine-type proteolytic activity that could be ... Plant physiology, Arabidopsis, molecular chaperone, protein degradation, protease, Clp/Hsp100, ClpP, stress response, antisense ... such as the rapid induction of specific molecular chaperones and proteases at the molecular level. Molecular chaperones mediate ...
Recombinant Protein and ATP-dependent protease ATPase Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and ... ATP-dependent protease ATPase subunit ClpY. ATP-dependent protease ATPase subunit ClpY ELISA Kit. ATP-dependent protease ATPase ... ATP-dependent protease ATPase subunit HslU. ATP-dependent protease ATPase subunit HslU ELISA Kit. ATP-dependent protease ATPase ... ATP-dependent protease ATPase subunit HslU1. ATP-dependent protease ATPase subunit HslU1 ELISA Kit. ATP-dependent protease ...
Recombinant Protein and ATP-dependent Clp protease proteolytic Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein ... Shop ATP-dependent Clp protease proteolytic ELISA Kit, ... ATP-dependent Clp protease proteolytic subunit. ATP-dependent ... ATP-dependent Clp protease proteolytic subunit 1. ATP-dependent Clp protease proteolytic subunit 1 ELISA Kit. ATP-dependent Clp ... ATP-dependent Clp protease proteolytic subunit 2. ATP-dependent Clp protease proteolytic subunit 2 ELISA Kit. ATP-dependent Clp ...
ATP-dependent Clp protease proteolytic subunit(clpP). It is produced in Yeast. High purity. Good price. ... ATP-dependent Clp protease proteolytic subunit(clpP). Recombinant Magnetococcus sp. ATP-dependent Clp protease proteolytic ... Recommended name: ATP-dependent Clp protease proteolytic subunit EC= 3.4.21.92 Alternative name(s): Endopeptidase Clp ... Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major ...
Lon and caseinolytic protease (Clp) are key enzymes responsible for the ATP-dependent degradation of cytosolic proteins in ... dependent proteases and ATP-independent peptidases during cytosolic protein degradation is conserved, with differences in the ... The roles of these proteases as essential enzymes and in the virulence of some organisms are discussed. ... The general pathway involving adenosine triphosphate (ATP)-dependent proteases and ATP-independent peptidases during cytosolic ...
A human mitochondrial ATP-dependent protease that is highly homologous to bacterial Lon protease.. Proc. Natl. Acad. Sci. U.S.A ... Lon (La) protease was the first ATP-dependent protease to be purified from E. coli [PMID: 9425059, PMID: 3042779, PMID: 8294008 ... ATP hydrolysis is not stoichiometrically linked with proteolysis in the ATP-dependent protease La from Escherichia coli.. J. ... Lon protease belongs to the S16 peptidase family and is an ATP-dependent serine protease that mediates the selective ...
Protease component of the Clp complex that cleaves peptides and various proteins in an ATP-dependent process. Has low peptidase ... HCA RNA Cell Line for ATP-dependent Clp protease proteolytic subunit, mitochondrial. ... encoded by this gene belongs to the peptidase family S14 and hydrolyzes proteins into small peptides in the presence of ATP and ...
The isolated proteolytic domain of Escherichia coli ATP-dependent protease Lon exhibits the peptidase activity. , FEBS letters ... The isolated proteolytic domain of Escherichia coli ATP-dependent protease Lon exhibits the peptidase activity. F S Rasulova N ... The isolated proteolytic domain of Escherichia coli ATP-dependent protease Lon exhibits the peptidase activity. FEBS Lett. 1998 ... Selective protein degradation is an energy-dependent process performed by high-molecular-weight proteases. The activity of ...
Purchase Recombinant Shewanella baltica ATP-dependent protease subunit HslV(hslV). It is produced in Yeast. High purity. Good ... Recombinant Shewanella baltica ATP-dependent protease subunit HslV(hslV). Recombinant Shewanella baltica ATP-dependent protease ... Recommended name: ATP-dependent protease subunit HslV EC= 3.4.25.2 Storage. The shelf life is related to many factors, storage ... Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.. ...
ATP-dependent proteases are crucial for cellular homeostasis. By degrading short-lived regulatory proteins, they play an ... ATP-dependent proteases are crucial for cellular homeostasis. By degrading short-lived regulatory proteins, they play an ... LON PROTEASE HOMOLOG, MITOCHONDRIAL. A, B, C, D, E, F. 207. Homo sapiens. Mutation(s): 0 Gene Names: LONP1, PRSS15. EC: 3.4.21 ... Structure of the proteolytic domain of the Human Mitochondrial Lon protease. *DOI: 10.2210/pdb2X36/pdb ...
Burkholderia ambifaria ATP-dependent protease subunit HslV (hslV) datasheet and description hight quality product and Backed by ... ATP-dependent protease peptidase subunit, ATP-dependent protease subunit HslV, ATP-dependent protease peptidase subunit. ... Burkholderia ambifaria ATP-dependent protease subunit HslV (hslV). Short name: Burkholderia ambifaria ATP-dependent protease ... Recombinant Burkholderia ambifaria ATP-dependent protease subunit HslV (hslV). Alternative names: ...
Visualizing ATP-dependent RNA translocation by the NS3 helicase from HCV. J Mol Biol, 405: 1139-1153.PubMedCentralPubMedGoogle ... A macrocyclic HCV NS3/4A protease inhibitor interacts with protease and helicase residues in the complex with its full-length ... The nonstructural protein 3 protease/helicase requires an intact protease domain to unwind duplex RNA efficiently. J Biol Chem ... Novel ATP-independent RNA annealing activity of the dengue virus NS3 helicase. PLoS One, 7: e36244.PubMedCentralPubMedGoogle ...
ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone ... Forms a hexameric ring that, in the presence of ATP, binds to fourteen ClpP subunits assembled into a disk-like structure with ... ATP-dependent Clp protease ATP-binding subunit ClpX - Also known as CLPX_BUCA5, clpX. ... ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone ...
Stenotrophomonas maltophilia ATP-dependent Clp protease ATP-binding subunit ClpX (clpX) datasheet and description hight quality ... ATP-dependent Clp protease ATP-binding subunit ClpX, ATP-dependent protease ATP-binding subunit ClpX, ATP-dependent protease ... Stenotrophomonas maltophilia ATP-dependent Clp protease ATP-binding subunit ClpX (clpX). Contact us. ... Stenotrophomonas maltophilia ATP-dependent Clp protease ATP-binding subunit ClpX (clpX). Short name: Stenotrophomonas ...
The clp stands for caseinolytic protease, which can degrade casein in vitro (12, 13). ATP-dependent protease ClpYQ is a type of ... Currently, few substrates have been identified for the ClpYQ protease in comparison with other ATP-dependent proteases (25⇓-27 ... E. coli has two major ATP-dependent proteases, which are Lon and Clp proteases. Lon is responsible for the degradation of ... and ATP-dependent proteases play a crucial role within this process. In Escherichia coli, ClpYQ is one of the primary ATP- ...
Together, our data demonstrate that phosphoarginine functions as a bona fide degradation tag for the ClpC-ClpP protease. This ... a general tagging system for the equivalent bacterial Clp proteases is not known. Here we describe the targeting mechanism of ... but it is unknown whether such a tagging system for the equivalent bacterial Clp proteases exists. Here, Tim Clausen and ... Goldberg, A. L. The mechanism and functions of ATP-dependent proteases in bacterial and animal cells. Eur. J. Biochem. 203, 9- ...
Induction by interferon-γ and contribution to ATP-dependent proteolysis. J. Biol. Chem. 275: 14336-14345. ... One such protease is furin, a member of the subtilisin family of serine proteases that is resident in the Golgi apparatus. ... Proteases in MHC Class I Presentation and Cross-Presentation Message Subject (Your Name) has forwarded a page to you from The ... Proteases in MHC Class I Presentation and Cross-Presentation. Kenneth L. Rock, Diego J. Farfán-Arribas and Lianjun Shen ...
5. ATP-dependent proteases in the chloroplast. Open this publication in new window or tab ,,ATP-dependent proteases in the ... In this book, we focus on a particular group of ATP-dependent proteases (Lon, Clp proteases, FtsH and HslUV) that function in ... ATP-dependent proteases constitute a unique proteolytic system. Although proteolysis is an exergonic process, these proteases ... ATP-dependent proteases are one of the largest groups of proteolytic enzymes found across all kingdoms of life and are ...
  • ATP-dependent Clp protease proteolytic subunit (ClpP) is an enzyme that in humans is encoded by the CLPP gene. (wikipedia.org)
  • Besides being important chaperones, many Clp/Hsp100 also participate in protein degradation by associating with the proteolytic subunit ClpP to form the Clp protease complex. (diva-portal.org)
  • Also known as ATP-dependent protease ATPase subunit HslU (Heat shock protein HslU) (Unfoldase HslU). (mybiosource.com)
  • Also known as ATP-dependent protease ATPase subunit HslU1 (Mitochondrial proteasome-like protease HslVU ATPase subunit 1). (mybiosource.com)
  • Also known as ATP-dependent Clp protease proteolytic subunit (Caseinolytic protease) (Endopeptidase Clp) (Heat shock protein F21.5) (Protease Ti). (mybiosource.com)
  • Also known as ATP-dependent Clp protease proteolytic subunit 6, chloroplastic (Endopeptidase ClpP6) (nClpP6) (nClpP1). (mybiosource.com)
  • Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. (cusabio.com)
  • FT CHAIN 1 174 ATP-dependent protease subunit HslV. (univ-lyon1.fr)
  • Clp is a Ser protease that separates its two essential functions in two different polypeptides: a small subunit, ClpP, containing the proteolytic active site, and a larger regulatory ATPase subunit, either ClpA or ClpX (for review, see Gottesman, 1996 ). (plantphysiol.org)
  • The Clp protease subunit P from Francisella tularensis assembled to two stacked heptameric rings that enclose a large chamber containing the protease active site including catalytic triad, Ser, His, and Glu/Asp. (csgid.org)
  • Color code reflects that for subunit A in (B,C) . The ribbon structure shows the D1 domain of a single protomer bound by a ATPγS molecule (PDB:4KO8). (frontiersin.org)
  • Flagellum-related protein FliT selectively increases ClpXP-dependent proteolysis of the FlhC subunit in the FlhD4C2 complex. (brenda-enzymes.org)
  • Binding of the RBD to 23S rRNA in the late stages of ribosome subunit maturation would position the ATP-binding duplex destabilization fragment of the protein for interaction with rRNA in the peptidyl transferase cleft of the subunit, allowing it to "melt out" unstable secondary structures and allow proper folding. (stanford.edu)
  • A gene on chromosome 7q22.1-q22.3 that encodes a 26S protease subunit involved in the ATP-dependent degradation of ubiquitinated proteins. (thefreedictionary.com)
  • Minimally, the system relies on a serine protease subunit, ClpP, and an AAA+ ATPase, such as ClpX, that recognizes and unfolds substrates for ClpP degradation. (asm.org)
  • A major goal of our research is to elucidate how many of the AAA+ subunits in the 19S base hydrolyze ATP or participate in substrate translocation, and what mechanisms are involved in subunit communication and coordination of activities in the hetero-hexameric ATPase ring. (berkeley.edu)
  • In several bacteria, such as E. coli, proteins tagged with the SsrA peptide (ANDENYALAA) encoded by tmRNA are digested by Clp proteases. (wikipedia.org)
  • The protein encoded by this gene belongs to the peptidase family S14 and hydrolyzes proteins into small peptides in the presence of ATP and magnesium. (wikipedia.org)
  • ClpP protease is a major contributor for mitochondrial protein quality control system and removing damaged or misfolded proteins in mitochondrial matrix. (wikipedia.org)
  • Proteases are enzymes that break down proteins. (sciencephoto.com)
  • Cleaves peptides in various proteins in a process that requires ATP hydrolysis. (uniprot.org)
  • Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. (uniprot.org)
  • Protease component of the Clp complex that cleaves peptides and various proteins in an ATP-dependent process. (uniprot.org)
  • Lon and caseinolytic protease (Clp) are key enzymes responsible for the ATP-dependent degradation of cytosolic proteins in Escherichia coli. (nih.gov)
  • Synergistic roles of HslVU and other ATP-dependent proteases in controlling in vivo turnover of sigma32 and abnormal proteins in Escherichia coli. (asm.org)
  • The overproduction of HslVU (ClpQY) protease markedly reduced the stability and accumulation of proUK and thus reduced the induction of heat shock proteins. (asm.org)
  • When the deltahslVU deletion was combined with another protease mutation (lon, clpP, or ftsH/hflB), the resulting multiple mutations caused higher stabilization of proUK and sigma32, enhanced synthesis of heat shock proteins, and temperature-sensitive growth. (asm.org)
  • Thus, a set of ATP-dependent proteases appear to play synergistic roles in the negative control of the heat shock response by modulating in vivo turnover of sigma32 as well as through degradation of abnormal proteins. (asm.org)
  • Molecular chaperones mediate the correct folding and assembly of polypeptides, as well as repair damaged protein structures caused by stress, while proteases remove otherwise non-functional and potentially cytotoxic proteins. (diva-portal.org)
  • Lon protease degrades transfer-messenger RNA-tagged proteins. (semanticscholar.org)
  • Lon protease belongs to the S16 peptidase family and is an ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins, as well as certain short-lived regulatory proteins. (ebi.ac.uk)
  • One of the most important functions for protease is to degrade the misfolding or functionless proteins. (mcponline.org)
  • Whereas ubiquitin marks eukaryotic proteins for proteasomal degradation, a general tagging system for the equivalent bacterial Clp proteases is not known. (nature.com)
  • Proteases play key roles in plants, maintaining strict protein quality control and degrading specific sets of proteins in response to diverse environmental and developmental stimuli. (diva-portal.org)
  • This complex is one of two parts of the ClpXP protease, which breaks down abnormally folded proteins. (medlineplus.gov)
  • The other part of the ClpXP protease, called the ClpX complex, unfolds the abnormal proteins and feeds them into the chamber formed by the ClpP complex, where they are broken down into small fragments. (medlineplus.gov)
  • FUNCTION: Acts as a processive, ATP-dependent zinc CC metallopeptidase for both cytoplasmic and membrane proteins. (univ-lyon1.fr)
  • Plastids contain tetradecameric Clp protease core complexes, with five ClpP Ser-type proteases, four nonproteolytic ClpR, and two associated ClpS proteins. (plantcell.org)
  • Adapter proteins, ClpS and SspB (stringent starvation protein B), interacting with the Clp chaperones, modulate substrate delivery to the Clp protease. (plantcell.org)
  • The availability of Arabidopsis thaliana and rice ( Oryza sativa ) genome sequences has permitted the identification and comparison of the repertoire of serine protease-like proteins in the two plant species. (biomedcentral.com)
  • Despite the differences in genome sizes between Arabidopsis and rice, we identified a very similar number of serine protease-like proteins in the two plant species (206 and 222, respectively). (biomedcentral.com)
  • The systematic analysis of the serine protease-like proteins in the two plant species has provided some insight into the possible functional associations of previously uncharacterised serine protease-like proteins. (biomedcentral.com)
  • The Clp protease is an ATP-dependent protease that cleaves a number of proteins, such as casein and albumin. (csgid.org)
  • Furthermore, we showed that the phylogenetic tree of FtsH proteases in phototrophic bacteria is similar to that for Type I and Type II reaction centre proteins. (springer.com)
  • ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. (genecards.org)
  • The degradation of cytoplasmatic proteins is an ATP-dependent process. (tum.de)
  • For example, the extracellular cysteine protease streptococcal erythrogenic toxin B (SPE B) degrades human extracellular matrix proteins ( 18 ) and activates human enzymes involved in host tissue remodeling ( 4 ). (asm.org)
  • ATP-dependent AAA+ proteases form ring-shaped assemblies that are composed of AAA+ proteins and an associated peptidase. (elifesciences.org)
  • AAA+ ( A TPase a ssociated with a variety of cellular a ctivities) proteins control a multitude of essential cellular activities by converting the energy derived from ATP hydrolysis into a mechanical force to remodel bound substrates ( Hanson and Whiteheart, 2005 ). (elifesciences.org)
  • AAA+ proteases are present in all branches of life and responsible for the energy-dependent degradation of most cytosolic proteins. (mit.edu)
  • Additionally they are capable of delivering damaged proteins to compartmentalized proteases. (cancer.gov)
  • We previously found that ICL is stabilized when a peroxisome-associated ubiquitin-conjugating enzyme and its membrane anchor are both mutated, suggesting that matrix proteins might exit the peroxisome for ubiquitin-dependent cytosolic degradation. (genetics.org)
  • The Clp proteins comprise an important and conserved protease system in bacteria. (asm.org)
  • In all cells, the degradation of intracellular proteins is highly specific and tightly regulated by ATP-dependent compartmental proteases. (berkeley.edu)
  • AAA (ATPase associated with various cellular activities) proteins remodel substrate proteins and protein complexes upon ATP hydrolysis. (portlandpress.com)
  • We have also investigated the roles of C. elegans p97 homologues in aggregation/disaggregation of polyglutamine repeats, and have found that p97 prevents filament formation of polyglutamine proteins in an ATP-independent fashion. (portlandpress.com)
  • Inducible protein degradation in Bacillus subtilis using heterologous peptide tags and adaptor proteins to target substrates to the protease ClpXP. (igem.org)
  • Before the discovery of the ubiquitin proteasome system, protein degradation in cells was thought to rely mainly on lysosomes , membrane-bound organelles with acidic and protease -filled interiors that can degrade and then recycle exogenous proteins and aged or damaged organelles. (wikipedia.org)
  • The 26S proteasome is the primary protease responsible for degrading misfolded membrane proteins in the endoplasmic reticulum. (biologists.org)
  • and other membrane proteins can be dislocated from the ER membrane and released en bloc into the cytosol. (biologists.org)
  • Enzyme ClpP is a highly conserved serine protease present throughout bacterial and also found in the mitochondria and chloroplasts of eukaryotic cells. (wikipedia.org)
  • A fully assembled Clp protease complex has a barrel-shaped structure in which two stacked ring of proteolytic subunits (ClpP or ClpQ) are either sandwiched between two rings or single-caped by one ring of ATPase-active chaperon subunits (ClpA, ClpC, ClpE, ClpX or ClpY). (wikipedia.org)
  • Defects in mitochondrial Clp proteases have been associated with the progression of neurodegenerative diseases while upregulation of ClpP proteases has been implicated in preventing premature aging. (wikipedia.org)
  • Regulation of cyclic lipopeptide biosynthesis in Pseudomonas fluorescens by the ClpP protease. (semanticscholar.org)
  • Global role for ClpP-containing proteases in stationary-phase adaptation of Escherichia coli. (semanticscholar.org)
  • Forms a hexameric ring that, in the presence of ATP, binds to fourteen ClpP subunits assembled into a disk-like structure with a central cavity, resembling the structure of eukaryotic proteasomes. (icr.ac.uk)
  • Together, our data demonstrate that phosphoarginine functions as a bona fide degradation tag for the ClpC-ClpP protease. (nature.com)
  • Perrault syndrome is caused by recessive mutations in CLPP, encoding a mitochondrial ATP-dependent chambered protease. (medlineplus.gov)
  • ClpP: a distinctive family of cylindrical energy-dependent serine proteases. (medlineplus.gov)
  • The plastid ClpPR protease complex in Arabidopsis thaliana consists of five catalytic ClpP and four noncatalytic ClpR subunits. (plantcell.org)
  • The catalytic chamber of the Clp protease core is enclosed in the barrel-shaped tetradecamer formed by two homoheptameric rings of ClpP peptidases, which are all encoded by a single gene ( Szyk and Maurizi, 2006 ). (plantcell.org)
  • Requirement of ATP hydrolysis for assembly of ClpA/ClpP complex, the ATP-dependent protease Ti in Escherichia coli. (yale.edu)
  • using this inhibitor we showed that the ClpP protease play important role in development of parasite apicoplast and thus it is essential for survival of the parasite. (icgeb.org)
  • The AAA+ chaperone ClpC with the peptidase ClpP forms a bacterial protease essential to virulence and stress resistance. (elifesciences.org)
  • ClpXP is a AAA+ protease that consists of the hexameric ClpX unfoldase and polypeptide translocase and the ClpP compartmental peptidase. (mit.edu)
  • ClpX binds a substrate by an unstructured degradation tag and then, by multiple rounds of ATP-binding and hydrolysis, unfolds and translocates the substrate into the proteolytic chamber of ClpP. (mit.edu)
  • New insights into the ATP-dependent Clp protease: Escherichia coli and beyond. (nih.gov)
  • Much of this directed protein turnover is performed by proteases that require ATP and, of those in bacteria, the Clp protease from Escherichia coli is one of the best characterized to date. (nih.gov)
  • Recombinant fragment corresponding to Escherichia coli ATP-dependent Clp protease adapter protein ClpS aa 1-105. (abcam.com)
  • We report here that a multicopy plasmid carrying the hslVU operon encoding a novel ATP-dependent protease inhibits the heat shock response induced by production of human prourokinase (proUK) in Escherichia coli. (asm.org)
  • The catalytic domain of Escherichia coli Lon protease has a unique fold and a Ser-Lys dyad in the active site. (semanticscholar.org)
  • Overproduction of the Lon protease triggers inhibition of translation in Escherichia coli: involvement of the yefM-yoeB toxin-antitoxin system. (semanticscholar.org)
  • Recent developments in the mechanistic enzymology of the ATP-dependent Lon protease from Escherichia coli: highlights from kinetic studies. (ebi.ac.uk)
  • Controlled high-level expression of the lon gene of Escherichia coli allows overproduction of Lon protease. (ebi.ac.uk)
  • ATP hydrolysis is not stoichiometrically linked with proteolysis in the ATP-dependent protease La from Escherichia coli. (ebi.ac.uk)
  • The isolated proteolytic domain of Escherichia coli ATP-dependent protease Lon exhibits the peptidase activity. (docphin.com)
  • Here, we obtained the proteolytic domain of Escherichia coli protease Lon by cloning the corresponding fragment of the lon gene in pGEX-KG, expression of the hybrid protein, and isolation of the proteolytic domain after hydrolysis of the hybrid protein with thrombin. (docphin.com)
  • In Escherichia coli , ClpYQ is one of the primary ATP-dependent proteases. (mcponline.org)
  • Regulated proteolysis by the essential FtsH protease in Escherichia coli . (springer.com)
  • Degradation of casein by the Escherichia coli AAA protease, FtsH, strictly requires ATP hydrolysis. (portlandpress.com)
  • The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. (mybiosource.com)
  • Protease Lon and its proteolytic domain differed in the efficiency and specificity of melittin hydrolysis. (docphin.com)
  • In conjunction with a large number of cofactors and adaptors, it couples ATP hydrolysis to segregation of polypeptides from immobile cellular structures such as protein assemblies, membranes, ribosome, and chromatin. (frontiersin.org)
  • The influence of the positvely and negatively charged residues near the gamma-phosphate of the nucleotide on nucleotide-binding, ATP-hydrolysis and proteolytic activity was studied by mutagenesis and biochemical experiments. (tum.de)
  • How do AAA+ ATPases convert the chemical energy of ATP binding and hydrolysis into mechanical unfolding and translocation? (mit.edu)
  • These proteases belong to the AAA+ ATPase family, whose characteristic feature is a structurally conserved ATPase domain that assembles into oligomeric rings and converts the energy of ATP binding/hydrolysis into conformational changes to perform mechanical work. (berkeley.edu)
  • In these complexes, the ATPases recognize appropriate protein substrates and harness ATP hydrolysis to drive the mechanical unfolding and the translocation of the polypeptide chain into a sequestered degradation chamber of the associated peptidase. (berkeley.edu)
  • Based on the homology with prokaryotic ATP-dependent unfoldases like ClpX, the base of the 19S cap is thought to mechanically unfold and translocate substrates in an ATP-hydrolysis dependent manner, but virtually nothing is known about the underlying molecular mechanisms. (berkeley.edu)
  • We do not yet understand how AAA+ unfoldases transduce the energy from ATP binding/hydrolysis into conformational changes for substrate translocation. (berkeley.edu)
  • We will use different spectroscopic methods to analyze the arrangement of structural elements within the 19S cap and their conformational changes upon ATP binding and hydrolysis. (berkeley.edu)
  • In the bacterial cytosol, ATP-dependent protein degradation is performed by several different chaperone-protease pairs, including ClpAP. (wikipedia.org)
  • Involved in the modulation of the specificity of the ClpAP-mediated ATP-dependent protein degradation. (abcam.com)
  • The general pathway involving adenosine triphosphate (ATP)-dependent proteases and ATP-independent peptidases during cytosolic protein degradation is conserved, with differences in the enzymes utilized, in organisms from different kingdoms. (nih.gov)
  • Selective protein degradation is an energy-dependent process performed by high-molecular-weight proteases. (docphin.com)
  • Furthermore, we validated that YbaB was successfully degraded by ClpYQ protease activity using ClpYQ in vitro and in vivo degradation assay. (mcponline.org)
  • Protease is responsible for protein degradation that can digest long protein chains into shorter fragments by splitting the peptide bonds ( 1 ). (mcponline.org)
  • The ATP-dependent protease of E. coli provides us an excellent example to understand the importance of protein degradation role in cell physiology. (mcponline.org)
  • Proteasomal protein degradation in Mycobacteria is dependent upon a prokaryotic ubiquitin-like protein. (nature.com)
  • Most notably, we describe a mutation in the ATP dependent protease HslUV that induces rapid degradation of σ32, and a mutation leading to increased levels of the house keeping σ70 that outcompete σ32 for binding to the RNA polymerase. (bireme.br)
  • ClpXP, an ATP-powered unfolding and protein-degradation machine. (medlineplus.gov)
  • Efficient degradation of damaged D1 during the repair of PSII is carried out by a set of dedicated FtsH proteases in the thylakoid membrane. (springer.com)
  • Three possible mechanisms for peroxisomal matrix protein degradation can be envisioned: degradation within the organelle by resident proteases, degradation of the entire organelle via autophagy, or retrotranslocation out of the organelle followed by cytosolic degradation. (genetics.org)
  • [1] However, work by Joseph Etlinger and Alfred Goldberg in 1977 on ATP-dependent protein degradation in reticulocytes , which lack lysosomes, suggested the presence of a second intracellular degradation mechanism. (wikipedia.org)
  • [7] It was then discovered that a previously identified protein associated with proteolytic degradation, known as ATP-dependent proteolysis factor 1 (APF-1), was the same protein as ubiquitin. (wikipedia.org)
  • [9] Later, the ATP -dependent proteolytic complex that was responsible for ubiquitin-dependent protein degradation was discovered and was called the 26S proteasome. (wikipedia.org)
  • Furthermore, overproduction of HslVU protease reduced sigma32 levels in strains that were otherwise expected to produce enhanced levels of sigma32 due either to the absence of Lon-ClpXP proteases or to the limiting levels of FtsH protease. (asm.org)
  • We were able to show that a metallo-protease belonging to the FtsH family is involved on the process in vitro. (diva-portal.org)
  • The transmembrane protein, FtsH, is the only known ATP-dependent protease responsible for this task. (bireme.br)
  • The structure and function of the ATPase and protease domains of FtsH have been previously characterized while the role of the FtsH periplasmic domain has not clearly identified. (bireme.br)
  • The proteolytic machinery of chloroplasts and mitochondria in Arabidopsis consists primarily of three families of ATP-dependent proteases, Clp, Lon, and FtsH, and one family of ATP-independent proteases, DegP. (plantphysiol.org)
  • These results suggest that, unlike previous expectations, the relative importance of different chloroplast protease isozymes, evidenced by mutant phenotypes at least in the FtsH family, is determined by their abundance, and not necessarily by different specific functions or specialized expression under certain conditions. (plantphysiol.org)
  • FtsH is the only essential ATP-dependent protease in E. coli . (plantphysiol.org)
  • as are the different forms of the FtsH protease. (plantphysiol.org)
  • A phylogenetic analysis of over 6000 FtsH protease sequences revealed that there are three major groups of FtsH proteases originating from gene duplication events in the last common ancestor of bacteria, and that the FtsH proteases involved in PSII repair make a distinct clade branching out before the divergence of FtsH proteases found in all groups of anoxygenic phototrophic bacteria. (springer.com)
  • We conclude that the phylogeny of FtsH proteases is consistent with an early origin of water oxidation chemistry. (springer.com)
  • Auxiliary functions in photosynthesis: the role of the FtsH protease. (springer.com)
  • Structure of Psb29/Thf1 and its association with the FtsH protease complex involved in photosystem II repair in cyanobacteria. (springer.com)
  • We have constructed several chimaeric proteases by exchanging domains of FtsH and its homologues from Caenorhabditis elegans mitochondria, and examined their ATPase and protease activities in vitro . (portlandpress.com)
  • May play the role of a master protease which is attracted to different substrates by different specificity factors such as ClpA or ClpX. (uniprot.org)
  • It directs the protease to specific substrates. (icr.ac.uk)
  • This work also successfully demonstrated that with the use of recognition element of a protease can successfully screen its substrates by indirect proteome chip screening assay. (mcponline.org)
  • However, the function and regulation of plant proteases is poorly understood primarily due to lack of identification of their physiological substrates. (biomedcentral.com)
  • Substrates are targeted to single soluble protease, the 26S proteasome, in eukaryotes and to a number of unrelated proteases is prokaryotes. (tum.de)
  • Substrates for AAA+ proteases are unfolded and translocated into a compartmental peptidase. (mit.edu)
  • Using β-casein as a substrate, plant mitochondria possessed an ATP-stimulated, serine-type proteolytic activity that could be strongly inhibited by antibodies specific for ClpX or ClpP2, suggesting an active ClpXP protease. (diva-portal.org)
  • Pharmacological inhibition of the ClpXP protease increases bacterial susceptibility to host cathelicidin antimicrobial peptides and cell envelope-active antibiotics. (semanticscholar.org)
  • 2007). 'Altered tethering of the SspB adaptor to the ClpXP protease causes changes in substrate delivery. (igem.org)
  • Fully functional Clp protease requires the participation of AAA+ ATPase. (wikipedia.org)
  • Below are the list of possible ATP-dependent protease ATPase products. (mybiosource.com)
  • Lon protease is an ATP-dependent Ser protease in which the catalytic and ATPase domains reside in a single polypeptide (for review, see Gottesman, 1996 ). (plantphysiol.org)
  • In this study, we demonstrate that two classes of metallopeptidases regulate OPA1 cleavage in the mitochondrial inner membrane: isoenzymes of the adenosine triphosphate (ATP)-dependent matrix AAA (ATPase associated with diverse cellular activities [ m -AAA]) protease, variable assemblies of the conserved subunits paraplegin, AFG3L1 and -2, and the ATP-independent peptidase OMA1. (rupress.org)
  • The assembly of the CC HslU/HslV complex is dependent on binding of ATP. (univ-lyon1.fr)
  • Its protease component HslV shares ~20% sequence similarity and a conserved fold with the 20S proteasome betha-subunits. (tum.de)
  • The protein substrate is then degraded by the ClpAP protease. (wikipedia.org)
  • These findings demonstrated the YbaB is a novel substrate of ClpYQ protease. (mcponline.org)
  • Figure 4: ClpCP protease activity towards a pArg-containing substrate protein. (nature.com)
  • Cleavage site selection within a folded substrate by the ATP-dependent lon protease. (proteopedia.org)
  • This study focuses on a molecular function of the plant mitochondrial inner membrane-embedded AAA protease (denoted i -AAA) FTSH4, providing its first bona fide substrate. (biologists.org)
  • Ring-forming AAA+ chaperones exert ATP-fueled substrate unfolding by threading through a central pore. (elifesciences.org)
  • One of several nuclear-encoded ClpPs (caseinolytic protease). (mybiosource.com)
  • This study characterized the function of the Arabidopsis ( Arabidopsis thaliana ) mitochondrial AAA-protease gene FtSH4 in regulating autophagy and senescence, finding that FtSH4 mediates WRKY-dependent salicylic acid ( SA ) accumulation and signaling. (plantphysiol.org)
  • While PCD in woody tissues shows the importance of vacuole proteases in the process, the senescence in leaves demonstrate to be a slower and more ordered mechanism starting in the chloroplast where the proteases there localized become important. (diva-portal.org)
  • The thylakoid membrane of clpr2-1 showed increased carotenoid content, partial inactivation of photosystem II, and upregulated thylakoid proteases and stromal chaperones, suggesting an imbalance in chloroplast protein homeostasis and a well-coordinated network of proteolysis and chaperone activities. (plantcell.org)
  • Another protease machinery characterized by our group is a cyanobacterial ClpAP serine protease system in the parasite. (icgeb.org)
  • Using the GFP targeting approach the ClpAP protease machinery was localized in the relict plastid in the parasite, the apicoplast. (icgeb.org)
  • Acyldepsipeptide antibiotics bind in the ClpA or ClpX binding-sites, rendering the enzyme ATP-independent and indiscriminate, thus killing cells. (uniprot.org)
  • 2009). 'Structures of asymmetric ClpX hexamers reveal nucleotide-dependent motions in a AAA+ protein-unfolding machine. (igem.org)
  • The enzyme is a homotetramer of 87kDa subunits, with one proteolytic and one ATP-binding site per monomer, making it structurally less complex than other known ATP-dependent proteases [ PMID: 3042779 ]. (ebi.ac.uk)
  • It exists as a heterodimer of ATP-binding regulatory A and catalytic P subunits, both of which are required for effective levels of protease activity in the presence of ATP. (csgid.org)
  • Our findings link distinct peptidases to constitutive and induced OPA1 processing and shed new light on the pathogenesis of neurodegenerative disorders associated with mutations in m -AAA protease subunits. (rupress.org)
  • The inner two rings are made of seven β subunits that contain three to seven protease active sites . (wikipedia.org)
  • In molecular biology, the ATP-dependent Clp protease adaptor protein ClpS is a bacterial protein. (wikipedia.org)
  • Molecular model of the bacterial enzyme HsIUV protease. (sciencephoto.com)
  • This signature defines the bacterial and eukaryotic lon proteases. (ebi.ac.uk)
  • Wang N, Gottesman S, Willingham MC, Gottesman MM, Maurizi MR. A human mitochondrial ATP-dependent protease that is highly homologous to bacterial Lon protease. (ebi.ac.uk)
  • Protease-induced protein regulation in bacterial cells is related to the antibiotic resistance, environmental resilience, and infectivity of bacteria ( 5 ). (mcponline.org)
  • Goldberg, A. L. The mechanism and functions of ATP-dependent proteases in bacterial and animal cells. (nature.com)
  • Plants have developed many protective mechanisms to survive and acclimate to stresses, such as the rapid induction of specific molecular chaperones and proteases at the molecular level. (diva-portal.org)
  • The lon protease from Mycobacterium smegmatis: molecular cloning, sequence analysis, functional expression, and enzymatic characterization. (ebi.ac.uk)
  • Our current research focuses on elucidating the mechanisms that underlie protein remodeling carried out by molecular chaperones and the role of chaperones in ATP-dependent proteolysis. (cancer.gov)
  • They act in conjunction with another ATP-dependent molecular chaperone, DnaK, in bacteria and Hsp70 in yeast. (cancer.gov)
  • The YTA10-12 complex, an AAA protease with chaperone-like activity in the inner membrane of mitochondria. (springer.com)
  • Across the species, highly conserved ATP-dependent proteases prevent malfunction of mitochondria through versatile activities. (biologists.org)
  • The ER stress response is subsequently transmitted to mitochondria and initiates a cascade of cellular events including: rise in cytosolic calcium levels, activation of VAD-FMK-binding proteases, dysregulation of mitochondrial development and suppression of protein translation machinery. (icgeb.org)
  • J.E. Walker, I.R. Collinson, M.J. Van Raaij, and M.J. Runswick , Structural Analysis of ATP Synthase from Bovine Heart Mitochondria. (elsevier.com)
  • J. Leighton , ATP-Binding Cassette Transporter in Saccharomyces cerevisiae Mitochondria. (elsevier.com)
  • Lon (La) protease was the first ATP-dependent protease to be purified from E. coli [ PMID: 9425059 , PMID: 3042779 , PMID: 8294008 , PMID: 8226758 ]. (ebi.ac.uk)
  • The E. coli Clp protease consists of a Ser-type protease tetradecameric core complex. (plantcell.org)
  • We made an important discovery in the field recently by demonstrating that Hsp90 of E. coli has innate ATP-dependent chaperone activity in vitro and that it functions synergistically with Hsp70 of E. coli, DnaK. (cancer.gov)
  • Endopeptidase Clp Clp protease family Varshavsky A (August 2011). (wikipedia.org)
  • This protein is an essential component to form the protein complex of Clp protease (Endopeptidase Clp). (wikipedia.org)
  • Proteolysis is a vital mechanism to regulate the cellular proteome in all kingdoms of life, and ATP-dependent proteases play a crucial role within this process. (mcponline.org)
  • Dr. Wickner's laboratory has contributed to the understanding of ATP-dependent protein machines essential for DNA replication, protein remodeling, and proteolysis. (cancer.gov)
  • The proteolysis is supported by either ATP[S] (adenosine 5′-[γ-thio]triphosphate) or ADP, as well as ATP. (portlandpress.com)
  • Zusätzlich wurden Untersuchungen an einem funktionellen Homolog der Tricorn-Protease, der Trilobed-Protease aus Pyrococcus furiosus durchgeführt. (tum.de)
  • Lon protease activity causes down-regulation of Salmonella pathogenicity island 1 invasion gene expression after infection of epithelial cells. (semanticscholar.org)
  • A heat-shock gene which encodes the ATP-dependent protease La. (ebi.ac.uk)
  • Maize contains a Lon protease gene that can partially complement a yeast pim1-deletion mutant. (ebi.ac.uk)
  • Atypical members could be identified in the plant genomes for Deg, Clp, Lon, rhomboid proteases and species-specific members were observed for the highly populated subtilisin and serine carboxypeptidase families suggesting multiple lateral gene transfers. (biomedcentral.com)
  • This gene encodes a mitochondrial matrix protein that belongs to the Lon family of ATP-dependent proteases. (genecards.org)
  • The rgg gene (also known as ropB ) is required for the expression of streptococcal erythrogenic toxin B (SPE B), an extracellular cysteine protease that contributes to virulence. (asm.org)
  • Pils and Schultz [ 1 ] argued that the large numbers of both inactive and active trypsin-like serine proteases, in both these species and their conservation in many other related species, indicated a gene expansion, and that the evolution of the inactive proteases and their new functions suggested that they were advantageous to insects. (portlandpress.com)
  • Contains a highly conserved catalytic triad of Ser-type proteases (Ser-His-Asp). (mybiosource.com)
  • Under such conditions, external environmental stimuli can activate the response systems of bacteria, including heat-shock and SOS responses, which can trigger the biosynthesis of the corresponding proteases, potentially aiding bacteria in overcoming unfavorable growth conditions ( 6 , 7 ). (mcponline.org)
  • The Clp protease system is well conserved in bacteria and important for protein turnover. (asm.org)
  • ATP-dependent specificity component of the Clp protease. (icr.ac.uk)
  • Structural evidence for regulation and specificity of flaviviral proteases and evolution of the Flaviviridae fold. (springer.com)
  • CATALYTIC ACTIVITY: ATP-dependent cleavage of peptide bonds with CC broad specificity. (univ-lyon1.fr)
  • One of these protease systems is the ClpQY system, an ATP dependent protease machinery, which is the prokaryotic counterpart of eukaryotic 20S proteasome. (icgeb.org)
  • The research of my lab focuses on the 26S proteasome, the major ATP-dependent protease in eukaryotic cells. (berkeley.edu)
  • Currently there are over 50 serine-protease families known as classified by MEROPS database[ 5 ], an information resource for peptidases and their inhibitors. (biomedcentral.com)
  • The availability of the complete genomic sequence of these two species renders it possible to carry out a comprehensive analysis of serine-protease families to gain insights into their function and to ascertain their evolutionary relationships. (biomedcentral.com)
  • The HslVU protease complex functions in mitochondrial DNA replication by regulating DNA helicase PIF2 protein levels. (mybiosource.com)
  • The light-harvesting complex of Photosystem II is very susceptible to protease attack during leaf senescence. (diva-portal.org)
  • The reduced accumulation of the ClpPRS protease complex led to a pale-green phenotype with delayed shoot development, smaller chloroplasts, decreased thylakoid accumulation, and increased plastoglobule accumulation. (plantcell.org)
  • This chaperone complex reversibly associates with the Clp protease complex. (plantcell.org)
  • Systematic comparative analysis of the available sequenced genomes of two model organisms led to the identification of an increasing number of protease genes, giving insights about protein sequences that are conserved in the different species, and thus are likely to have common functions in them and the acquisition of new genes, elucidate issues concerning non-functionalization, neofunctionalization and subfunctionalization. (diva-portal.org)
  • Analysis of prokaryotic and eukaryotic genomes reveals that the number of genes encoding the aforementioned proteases has increased during evolution. (plantphysiol.org)
  • Taken together, these results suggest that the mitochondrial ATP-dependent protease FtSH4 may regulate the expression of WRKY genes by modifying the level of reactive oxygen species and the WRKY transcription factors that control SA synthesis and signaling in autophagy and senescence. (plantphysiol.org)
  • The expression of several WRKY genes is up-regulated in response to ROS or ROS -generating stimuli, imbalances in redox homeostasis, and endogenous ROS -dependent processes such as senescence ( Ulker and Somssich, 2004 ). (plantphysiol.org)
  • Transcription of chaperone and protease genes (ATP-dependent Clp and La proteases, and DnaK) were also elevated in D. vulgaris. (unt.edu)
  • Durch eine Mutagenesestudie an der ATP-Bindetasche von HslU wurde der Einfluß der positiv und negativ geladenen Reste auf die ATP-Hydrolyse/Bindung von HslU und der Proteolyseaktivitäten von HslVU untersucht. (tum.de)
  • A surprising link emerged with the discovery of the ATP-dependent protease HslVU. (tum.de)
  • The roles of these proteases as essential enzymes and in the virulence of some organisms are discussed. (nih.gov)
  • Serine proteases are one of the largest groups of proteolytic enzymes found across all kingdoms of life and are associated with several essential physiological pathways. (biomedcentral.com)
  • Serine proteases are one of the largest groups of proteolytic enzymes involved in numerous regulatory processes. (biomedcentral.com)
  • Catalytically inactive enzymes (also known as pseudoproteases, protease homologues or paralogues, non-peptidase homologues, non-enzymes and pseudoenzymes) have traditionally been hypothesized to act as regulators of their active homologues. (portlandpress.com)
  • Enzymes that help such reactions are called proteases . (wikipedia.org)
  • The RNA helicase, nucleotide 5′-triphosphatase, and RNA 5′-triphosphatase activities of Dengue virus protein NS3 are Mg2+-dependent and require a functional Walker B motif in the helicase catalytic core. (springer.com)
  • Plants that are lacking functional FTSH4 protease are characterized by significantly enhanced capacity of preprotein import through the TIM17:23-dependent pathway. (biologists.org)
  • Functional analysis indicates that this conserved residue in AAA proteases is involved in threading unfolded polypeptides. (portlandpress.com)
  • Structure of the catalytic domain of the human mitochondrial Lon protease: proposed relation of oligomer formation and activity. (proteopedia.org)
  • The homologs of these energy (ATP or GTP)-dependent proteases were also found in eukaryotes indicating the similar regulation cascades between prokaryotes and eukaryotes ( 5 ). (mcponline.org)
  • The analysis reveals some domain architectures unique to either or both of the plant species and some inactive proteases, like in rhomboids and Clp proteases, which could be involved in chaperone function. (biomedcentral.com)
  • We assessed the role of mitochondrial protection mechanisms (ATP-dependent and ATP-independent mitochondrial proteases, and antioxidants) in tolerance to intermittent hypoxia or anoxia in three species of marine bivalves: the hypoxia tolerant hard clams ( Mercenaria mercenaria ) and oysters ( Crassostrea virginica ), and a hypoxia-sensitive subtidal scallop ( Argopecten irradians ). (biologists.org)
  • In clams and oysters, mitochondrial tolerance to hypoxia (18 h at 5% O 2 ), anoxia (18 h at 0.1% O 2 ) and subsequent reoxygenation was associated with the ability to maintain the steady-state activity of ATP-dependent and ATP-independent mitochondrial proteases and an anticipatory upregulation of the total antioxidant capacity (TAOC) under the low oxygen conditions. (biologists.org)
  • In contrast, hypoxia/anoxia and reoxygenation strongly suppressed activity of the ATP-dependent mitochondrial proteases in hypoxia-sensitive scallops. (biologists.org)
  • These findings highlight a key role of mitochondrial proteases in protection against hypoxia-reoxygenation stress and adaptations to frequent oxygen fluctuations in intertidal mollusks. (biologists.org)
  • Interestingly, it has been found that some chimaeras are able to degrade casein in an ATP-independent manner. (portlandpress.com)
  • The Brucella abortus Lon functions as a generalized stress response protease and is required for wild-type virulence in BALB/c mice. (ebi.ac.uk)
  • PIM1 encodes a mitochondrial ATP-dependent protease that is required for mitochondrial function in the yeast Saccharomyces cerevisiae. (ebi.ac.uk)
  • CRBN encodes a protein related to the Lon protease protein family. (antikoerper-online.de)
  • All mutations reduced the activity of the heat shock sigma factor σ32, demonstrating that the DnaK-dependent inactivation of σ32 is a growth requirement. (bireme.br)
  • DnaK and GroEL) and ATP-dependent proteases (e.g. (asm.org)
  • Taken together, with the observation that FTSH4 prevents accumulation of Tim17-2, our data point towards the role of this i -AAA protease in the regulation of mitochondrial biogenesis in plants. (biologists.org)
  • Our group is working on several parasite proteases that may be involved in organelle biogenesis and parasite survival. (icgeb.org)
  • Visualizing ATP-dependent RNA translocation by the NS3 helicase from HCV. (springer.com)
  • In addition, the protease-induced protein regulation is very important in the wide-range organism. (mcponline.org)
  • Similarities and differences between the proteases expressed in different species may give valuable insights into their physiological roles and evolution. (diva-portal.org)
  • To explore this hypothesis, we used an in silico approach to evaluate the relationship of pathogenic potential and the divergence of the SigB-dependent general stress response within the B. cereus sensu lato group, since SigB has been demonstrated to support pathogenesis in Bacillus , Listeria and Staphylococcus species. (biomedcentral.com)
  • Andersson B and Aro E-M (1997) Proteolytic activities and proteases of plant chloroplasts. (springer.com)