Calpain: 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.Adenosine Triphosphate: 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.Adenosine Triphosphatases: 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.Endopeptidases: A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.Peptide Hydrolases: Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group include EXOPEPTIDASES and ENDOPEPTIDASES.Kinetics: The rate dynamics in chemical or physical systems.Calcium: 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.Blood Platelets: Non-nucleated disk-shaped cells formed in the megakaryocyte and found in the blood of all mammals. They are mainly involved in blood coagulation.Molecular Weight: The sum of the weight of all the atoms in a molecule.Electrophoresis, Polyacrylamide Gel: Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.Enzyme Activation: 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.Protease Inhibitors: Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES).HIV Protease: 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.Serine Endopeptidases: Any member of the group of ENDOPEPTIDASES containing at the active site a serine residue involved in catalysis.Molecular Sequence Data: 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.Protease La: 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.Amino Acid Sequence: 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.Cysteine Proteases: A subclass of peptide hydrolases that depend on a CYSTEINE residue for their activity.ATP-Dependent Proteases: 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.Cysteine Endopeptidases: 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.Protease Nexins: Extracellular protease inhibitors that are secreted from FIBROBLASTS. They form a covalent complex with SERINE PROTEASES and can mediate their cellular internalization and degradation.Serine Proteinase Inhibitors: Exogenous or endogenous compounds which inhibit SERINE ENDOPEPTIDASES.Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.Hydrolysis: The process of cleaving a chemical compound by the addition of a molecule of water.Cell Line: Established cell cultures that have the potential to propagate indefinitely.Mutation: 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.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Protein Binding: 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, Cultured: 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.Recombinant Proteins: Proteins prepared by recombinant DNA technology.Escherichia coli: 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.Hydrogen-Ion Concentration: 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)Signal Transduction: 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.Bacterial Proteins: Proteins found in any species of bacterium.Models, Molecular: Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.Cysteine Proteinase Inhibitors: Exogenous and endogenous compounds which inhibit CYSTEINE ENDOPEPTIDASES.Sequence Homology, Amino Acid: The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.Cathepsins: 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 Diphosphate: Adenosine 5'-(trihydrogen diphosphate). An adenine nucleotide containing two phosphate groups esterified to the sugar moiety at the 5'-position.Cloning, Molecular: 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.Time Factors: Elements of limited time intervals, contributing to particular results or situations.Trypsin: 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.ATP Synthetase Complexes: Multisubunit enzyme complexes that synthesize ADENOSINE TRIPHOSPHATE from energy sources such as ions traveling through channels.Protein Processing, Post-Translational: 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.Ubiquitin-Specific Proteases: 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.Endopeptidase Clp: 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.Membrane 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.Apoptosis: 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.Phosphorylation: The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.Metalloendopeptidases: ENDOPEPTIDASES which use a metal such as ZINC in the catalytic mechanism.Subtilisins: A family of SERINE ENDOPEPTIDASES isolated from Bacillus subtilis. EC 3.4.21.-Cell Membrane: The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.RNA, Messenger: 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.Chymotrypsin: 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.Oligopeptides: Peptides composed of between two and twelve amino acids.Models, Biological: 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.Aspartic Acid Endopeptidases: A sub-subclass of endopeptidases that depend on an ASPARTIC ACID residue for their activity.Dose-Response Relationship, Drug: The relationship between the dose of an administered drug and the response of the organism to the drug.Carrier Proteins: Transport proteins that carry specific substances in the blood or across cell membranes.Recombinant Fusion Proteins: 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.Mice, Inbred C57BLPeptide Fragments: Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.Rabbits: 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.Proteolysis: 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.Mutagenesis, Site-Directed: Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.Sequence Alignment: 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.Pepstatins: N-acylated oligopeptides isolated from culture filtrates of Actinomycetes, which act specifically to inhibit acid proteases such as pepsin and renin.Mitochondria: 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)Mice, Knockout: 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.Temperature: 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.Cattle: 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.Enzyme Inhibitors: Compounds or agents that combine with an enzyme in such a manner as to prevent the normal substrate-enzyme combination and the catalytic reaction.Magnesium: 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.Transfection: 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.Protein Structure, Tertiary: 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.Transcription, Genetic: The biosynthesis of RNA carried out on a template of DNA. The biosynthesis of DNA from an RNA template is called REVERSE TRANSCRIPTION.Blotting, Western: 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.Enzyme Precursors: Physiologically inactive substances that can be converted to active enzymes.Peptides: 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.Structure-Activity Relationship: 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.DNA-Binding Proteins: 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.Serpins: 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.Catalytic Domain: The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.Plasmids: 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.Catalysis: The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.Pancreatic Elastase: 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.Mitochondrial Proton-Translocating ATPases: 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.HeLa Cells: 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.Gene Expression Regulation: 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 ...
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 ...
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.
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…
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…
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 ...
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. ...
The mitochondrial protein AFG3L2 forms homo-oligomeric and hetero-oligomeric complexes with paraplegin in the inner mitochondrial membrane, named m-AAA proteases. These complexes are in charge of quality control of misfolded proteins and participate in the regulation of OPA1 proteolytic cleavage, required for mitochondrial fusion. Mutations in AFG3L2 cause spinocerebellar ataxia type 28 and a complex neurodegenerative syndrome of childhood. In this study, we demonstrated that the loss of AFG3L2 in mouse embryonic fibroblasts (MEFs) reduces mitochondrial Ca2+ uptake capacity. This defect is neither a consequence of global alteration in cellular Ca2+ homeostasis nor of the reduced driving force for Ca2+ internalization within mitochondria, since cytosolic Ca2+ transients and mitochondrial membrane potential remain unaffected. Moreover, experiments in permeabilized cells revealed unaltered mitochondrial Ca2+ uptake speed in Afg3l2−/− cells, indicating the presence of functional Ca2+ uptake ...
Proteasome subunit beta type ; The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity (245 aa ...
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Regulatory particle non-ATPase 12A; Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. May help to control the degradation of one or more factors that repress cytokinin signaling. Plays an important role for balancing cell expansion with cell proliferation rates during shoot development (267 aa ...
We see that the first time Enterprise if found, it is in county Coffee in lat/lon:31.31/-85.85. The second hit is for county Chilton with lat/lon:32.73/-86.62. You can now use the Google Maps button (or press TAB key) while the lat/lon subentry is selected to see where this city is in both cases. From this it will be clear for example that one is a hamlet, not really a city, while the first is a real city. So now, select the second lat/lon entry, and delete it by pressing the DEL key. Do the same for the second county entry. In case google maps did not allow you to determine which is the correct city, you can double click on the city to open the Place Dialog (Warning: this will preenter the data of the Place Completion tool. So hit cancel here if you want to exit without these changes done). In this dialog the references tab allows you to navigate to all events coupled to this place. This will give you extra information you might use to decide which of the two found places is the correct ...
We see that the first time Enterprise if found, it is in county Coffee in lat/lon:31.31/-85.85. The second hit is for county Chilton with lat/lon:32.73/-86.62. You can now use the Google Maps button (or press TAB key) while the lat/lon subentry is selected to see where this city is in both cases. From this it will be clear for example that one is a hamlet, not really a city, while the first is a real city. So now, select the second lat/lon entry, and delete it by pressing the DEL key. Do the same for the second county entry. In case google maps did not allow you to determine which is the correct city, you can double click on the city to open the Place Dialog (Warning: this will preenter the data of the Place Completion tool. So hit cancel here if you want to exit without these changes done). In this dialog the references tab allows you to navigate to all events coupled to this place. This will give you extra information you might use to decide which of the two found places is the correct ...
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0035] First, suitable cell enlargers according to the best mode are not particularly limited, as long as (1) at predetermined concentrations, they are disposed to inhibit or suppress cell division to allow microbial cells to enlarge, and (2) when the concentrations are lowered, they will be disposed to lose the action of inhibiting or suppressing cell division, exerting no adverse effect on normal proliferation and other functions (reversible), example of which may include cell division inhibitors for terminating cell division, for example, agents having inhibitory action on enzymes involved in cell division (such as antibiotics and agricultural chemicals). Specific examples of agents having such properties may include pyridonecarboxylic acid-based antibiotics (for example, nalidixic acid, pipemidic acid and piromidic acid). When the cell enlargers are used, cells grow to lengths or sizes approximately three to four times as large as the normal sizes, for example. Here, different types of cell ...
How to purify unstable protein? - posted in Protein Expression and Purification: I am facing problem with purification of a mutant protein by E. coli expression system. Expression of that soluble protein is good and like as wild type. But after purification of that protein by Ni-NTA column, when I tried by gelfiltration it was denatured. How can I solved this problem? I have purified wild type with same procedure without any problem. Please suggest me. Thanks in advance for your suggestions.
HRQOL: TMZ vs PCB for recurrent GBM: Osoba et al. JCO 2000. TMZ in Newly Diagnosed GBM: Stupp NEJM 2005. Stupp NEJM 2005. PFS Benefit. OS Benefit ... – A free PowerPoint PPT presentation (displayed as a Flash slide show) on PowerShow.com - id: d6b3-YmE1M
lon: Daren Fletcher is a registered osteopath in Victoria, Kensington and Ealing. However, Daren\s Find an Osteopath profile has never been updated. Oste...
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sp:DNLI1_XENLA] lig1.L, lig1, lig1.S, ligI; ligase I, DNA, ATP-dependent L homeolog; K10747 DNA ligase 1 [EC:6.5.1.1 6.5.1.6 6.5.1.7] ...
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The discovery that expression of API2-MALT1 results in constitutive activation of the canonical NF-κB pathway (4, 5) led to numerous investigations of the role of MALT1 as a regulator of the NF-κB family of transcription factors. MALT1 binds to the adaptor protein BCL10 and synergizes with BCL10 in promoting canonical NF-κB activation (4, 5). Notably, MALT1 and BCL10 can each be deregulated via the recurrent t(14;18)(q32;q21) and t(1;14)(p22;q32) translocations in MALT lymphoma, respectively, because these translocations bring the MALT1 or BCL10 gene under the control of the immunoglobulin (Ig) heavy-chain gene enhancer, thus leading to inappropriately enhanced expression (6). In addition to its caspase-like proteolytic domain, MALT1 contains an amino-terminal death domain and 3 Ig-like protein-protein interaction domains (Fig. 1A). BCL10 binds to a region of MALT1 that comprises the death domain and first Ig domain, and this interaction induces the oligomerization of MALT1 (4, 7). MALT1 ...
Expression of AFG3L2 (SCA28, SPAX5) in fallopian tube tissue. Antibody staining with HPA004479 and HPA004480 in immunohistochemistry.
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Homeless and savagely beaten, Amy Mair sits waiting in a police interrogation room. She witnessed the murder of a friend and the police want to know more. But...
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With China and her island province Taiwan wading with utter belligerence within our watery borders, perhaps it is worth our while to think of times-now lon
From the Diary as of 10/16 - 10/18/2011 10/16 I weighed Lucky today: he is on 303 gr - so he lost a little bit more but not too much - a good start for a recovery. Today he received his last Baytril #7 and Flagyl #3. From now on I will give him the…
The results we have shown here and in a previous report (Sauret-Güeto et al., 2006) confirm a strong and specific influence of plastid cues in the regulation of the MEP pathway for isoprenoid biosynthesis. Evidence provided in this work unveils a mechanism for such regulation involving the participation of the plastidic Clp protease complex. Impaired expression of the plastid genome in rif1, rif10, and CAP-treated Col seedlings unexpectedly resulted in increased levels of the plastome-encoded ClpP1 subunit of the catalytic ClpPR core of the complex (Figure 7). It is possible that ClpP1 levels are modulated not only by their biosynthetic rate but also by a regulatory feedback mechanism at the posttranslational level. As a result, a defective production of ClpP1 in the first stages of plastid development might result in an altered proportion of subunits within the ClpPR core and an insufficient Clp protease activity, which in turn might lead to the observed upregulation of ClpP1 levels as a ...
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... (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, W.P.; Maurizi, M.R. ( ... Maurizi, M.R.; Thompson, M.W.; Singh, S.K.; Kim, S.-H. (1994). "Endopeptidase Clp: the ATP-dependent Clp protease from ... "The ATP-dependent Clp protease of Escherichia coli. Sequence of clpA and identification of a Clp-specific substrate". J. Biol. ...
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 (Apr 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 ...
ATP-dependent serine proteinase, lon proteinase, protease La, proteinase La, ATP-dependent lon proteinase, ATP-dependent ... Larimore, F.S.; Waxman, L.; Goldberg, A.L. (1982). "Studies of the ATP-dependent proteolytic enzyme, protease La, from ... A heat-shock gene which encodes the ATP-dependent protease La". J. Biol. Chem. 263: 11718-11728. PMID 3042779. Endopeptidase La ... gene lon protease, gene lon proteins, PIM1 protease, PIM1 proteinase, serine protease La) is an enzyme. This enzyme catalyses ...
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 ...
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: ...
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 ...
"A mutation in a novel ATP-dependent Lon protease gene in a kindred with mild mental retardation". Neurology. 63 (10): 1927-31. ...
1996). HslV-HslU: A novel ATP-dependent protease complex in Escherichia coli related to the eukaryotic proteasome. Proc Natl ... 2005). Nucleotide-dependent substrate recognition by the AAA+ HslUV protease. Nat Struct Mol Biol 12(3):245-51.. ... Like the proteasome, hslU must bind ATP in a magnesium-dependent manner before substrate binding and unfolding can occur. ... The hslV protein is a protease and the hslU protein is an ATPase; the two form a symmetric assembly of four stacked rings, ...
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 ... Once translated, the polyprotein is cleaved by a combination of viral and host proteases to release mature polypeptide products ... Nevertheless, cellular post-translational modification is dependent on the presence of a poly-A tail; therefore this process is ... RNA binding affinity is reduced by the presence of ATP or GTP and enhanced by S-adenosyl methionine. This protein also encodes ...
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 are classified in as non-peptidase homologues and unassigned peptidases in MEROPS peptidase family S16 (lon protease ... both RecA strand transferase and lon protease. ...
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 ...
ATP-dependent HslV-HslU proteinase, caseinolytic protease X, caseinolytic proteinase X, ClpXP ATP-dependent protease, ClpXP ... Kanemori, M.; Nishihara, K.; Yanagi, H.; Yura, T. (1997). "Synergistic roles of HslVU and other ATP-dependent proteases in ... by the ATP-dependent HslVU protease from Escherichia coli". FEBS Lett. 553: 351-354. doi:10.1016/s0014-5793(03)01044-5. PMID ... protease HslVU, proteinase HslUV) is an enzyme. This enzyme catalyses the following chemical reaction ATP-dependent cleavage of ...
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 ATP-dependent substrate specificity component of the ClpP-ClpX protease, is a novel molecular chaperone". EMBO J. 14: 1867- ... Blond-Elquindi, S.; Fourie, A.M.; Sambrook, J.F.; Gething, M.J. (1993). "Peptide-dependent stimulation of the ATPase activity ... 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: 9406-9412. ...
The predicted structure is Chain A, crystal structure analysis of Clpb, a protein that encodes an ATP-dependent protease 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. ClpX is an ATP-dependent chaperone that can ... During protease Clp complex assembly, the ClpX subunits form a hexameric ring structure. According to the orientation of ClpX ... This protein is a member of the family of AAA Proteins (AAA+ ATPase) and is to form the protein complex of Clp protease ( ...
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. ... Subsequent changes in ATP concentrations hydrolyze the bonds between the protein and HSP60 which signals the protein to exit ... Chaperonin 10 aids HSP60 in folding by acting as a dome-like cover on the ATP active form of HSP60. This causes the central ...
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 ... Krinke, L.; Wulff, D.L. (1990). "RNase III-dependent hydrolysis of λcII-O gene mRNA mediated by λ OOP antisense RNA". Genes Dev ... This tag is recognized by host proteases HflA and HflB, cause rapid proteolysis cII. Although the C-terminal tag is still ...
... encoding enzyme ATP-dependent Clp protease ATP-binding subunit clpX-like, mitochondrial COMMD4: encoding protein COMM domain- ... encoding enzyme Sentrin-specific protease 8 SERF2: encoding protein Small EDRK-rich factor 2 SLC24A5: the gene responsible for ... encoding protein High mobility group protein 20A IDDM3 encoding protein Insulin dependent diabetes mellitus 3 IMP3: encoding ...
... 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 9 MeSH D08.811.913.696.620.682.700.200.323 --- cyclin-dependent kinase 2 MeSH D08.811.913.696.620.682. ... 700.200.451 --- cyclin-dependent kinase 4 MeSH D08.811.913.696.620.682.700.200.515 --- cyclin-dependent kinase 6 MeSH D08.811. ... cyclin-dependent kinase 5 MeSH D08.811.913.696.620.682.700.646.500.750 --- cyclin-dependent kinase 2 MeSH D08.811.913.696. ...
... 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 ... RpoS-dependent genes involved in changes in cell membrane permeability and general cell morphology mostly belong to the osm ... Discovery of RpoS-dependent virulence genes in Salmonella are consistent with RpoS as a general regulator of the stress ...
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 ...
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 ...
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; ...
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 ...
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) ... Plants that are lacking functional FTSH4 protease are characterized by significantly enhanced capacity of preprotein import ... The plant i-AAA protease controls the turnover of an essential mitochondrial protein import component ...
Histone H1 subtypes differentially modulate chromatin condensation without preventing ATP-dependent remodeling by SWI/SNF or ... We previously established that the serine protease factor VII-activating protease (FSAP) is activated in serum upon incubation ... Factor seven activating protease (FSAP): does it activate factor VII? J Thromb Haemost. 2012;10(5):859-866. ... Factor VII-activating protease is activated in multiple trauma patients and generates anaphylatoxin C5a. J Immunol. 2012;188(6 ...
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.
... 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, Alexander (2011-08-01). "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 ...
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- ...
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): ...
ATP-dependent Clp protease ATP-binding subunit ClpA. Clostridium colicanis DSM 13634 ... ATP-dependent Clp protease ATP-binding subunit ClpA. Clostridium thermopalmarium DSM 5974 ... ATP-dependent Clp protease subunit A (ClpA)Imported. Automatic assertion inferred from database entriesi ... tr,O83779,O83779_TREPA ATP-dependent Clp protease subunit A (ClpA) OS=Treponema pallidum (strain Nichols) OX=243276 GN=clpA2 PE ...
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 ...
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.. ...
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: ...
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 ...
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 ...
ATP-dependent protease homolog; cyc, cyclase; dh, dehydratase; hyd, hydroxylase; kr, ketoreductase; ks, β-ketoacyl synthase; mt ... on which amino acid substrates are first activated by ATP to the corresponding adenylate. The unstable adenylate is ...
ATP-dependent metalloprotease FtsH; KW ATP-binding; Cell inner membrane; Cell membrane; Complete proteome; KW Hydrolase; ... Membrane; Metal-binding; Metalloprotease; KW Nucleotide-binding; Protease; Signal; Transmembrane; KW Transmembrane helix; Zinc ... 3, Last annotation update) DE RecName: Full=ATP-dependent zinc metalloprotease FtsH; EC=3.4.24 -;Flags: DE Precursor; (MARMS_1. ... CC Genomes CC -!- ANNOTATIONS ORIGIN:A6VU22_MARMS CC -!- FUNCTION: Acts as a processive, ATP-dependent zinc CC metallopeptidase ...
  • Lon protease activity causes down-regulation of Salmonella pathogenicity island 1 invasion gene expression after infection of epithelial cells. (semanticscholar.org)
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