Cold Shock Proteins and Peptides: Cellular proteins and peptides that are induced in response to cold stress. They are found in a broad variety of prokaryotic and eukaryotic organisms.Cold Temperature: An absence of warmth or heat or a temperature notably below an accustomed norm.Heat-Shock Proteins: Proteins which are synthesized in eukaryotic organisms and bacteria in response to hyperthermia and other environmental stresses. They increase thermal tolerance and perform functions essential to cell survival under these conditions.Bacterial Proteins: Proteins found in any species of bacterium.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.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.Gene Expression Regulation, Bacterial: Any of the processes by which cytoplasmic or intercellular factors influence the differential control of gene action in bacteria.Thermotoga maritima: A rod-shaped bacterium surrounded by a sheath-like structure which protrudes balloon-like beyond the ends of the cell. It is thermophilic, with growth occurring at temperatures as high as 90 degrees C. It is isolated from geothermally heated marine sediments or hot springs. (From Bergey's Manual of Determinative Bacteriology, 9th ed)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.Freezing: Liquids transforming into solids by the removal of heat.HSP70 Heat-Shock Proteins: A class of MOLECULAR CHAPERONES found in both prokaryotes and in several compartments of eukaryotic cells. These proteins can interact with polypeptides during a variety of assembly processes in such a way as to prevent the formation of nonfunctional structures.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.Bacillus subtilis: A species of gram-positive bacteria that is a common soil and water saprophyte.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.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Escherichia coli Proteins: Proteins obtained from ESCHERICHIA COLI.Cold-Shock Response: A constellation of responses that occur when an organism is exposed to excessive cold. In humans, a fall in skin temperature triggers gasping, hypertension, and hyperventilation.Shock, Septic: Sepsis associated with HYPOTENSION or hypoperfusion despite adequate fluid resuscitation. Perfusion abnormalities may include, but are not limited to LACTIC ACIDOSIS; OLIGURIA; or acute alteration in mental status.Adaptation, Physiological: The non-genetic biological changes of an organism in response to challenges in its ENVIRONMENT.Protein Folding: Processes involved in the formation of TERTIARY PROTEIN STRUCTURE.Shock: A pathological condition manifested by failure to perfuse or oxygenate vital organs.HSP90 Heat-Shock Proteins: A class of MOLECULAR CHAPERONES whose members act in the mechanism of SIGNAL TRANSDUCTION by STEROID RECEPTORS.RNA, Bacterial: Ribonucleic acid in bacteria having regulatory and catalytic roles as well as involvement in protein synthesis.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.Heat-Shock Response: A constellation of responses that occur when an organism is exposed to excessive heat. Responses include synthesis of new proteins and regulation of others.HSP27 Heat-Shock Proteins: A subfamily of small heat-shock proteins that function as molecular chaperones that aid in refolding of non-native proteins. They play a protective role that increases cellular survival during times of stress.RNA-Binding Proteins: Proteins that bind to RNA molecules. Included here are RIBONUCLEOPROTEINS and other proteins whose function is to bind specifically to RNA.Hot Temperature: Presence of warmth or heat or a temperature notably higher than an accustomed norm.Chaperonin 60: A group I chaperonin protein that forms the barrel-like structure of the chaperonin complex. It is an oligomeric protein with a distinctive structure of fourteen subunits, arranged in two rings of seven subunits each. The protein was originally studied in BACTERIA where it is commonly referred to as GroEL protein.Models, Molecular: Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.Protein Conformation: The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).Carrier Proteins: Transport proteins that carry specific substances in the blood or across cell membranes.Protein Structure, Secondary: The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to alpha helices, beta strands (which align to form beta sheets) or other types of coils. This is the first folding level of protein conformation.Peptide Fragments: Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.HSP72 Heat-Shock Proteins: Stress-inducible members of the heat-shock proteins 70 family. HSP72 heat shock proteins function with other MOLECULAR CHAPERONES to mediate PROTEIN FOLDING and to stabilize pre-existent proteins against aggregation.Shock, Hemorrhagic: Acute hemorrhage or excessive fluid loss resulting in HYPOVOLEMIA.Common Cold: A catarrhal disorder of the upper respiratory tract, which may be viral or a mixed infection. It generally involves a runny nose, nasal congestion, and sneezing.Peptide Library: A collection of cloned peptides, or chemically synthesized peptides, frequently consisting of all possible combinations of amino acids making up an n-amino acid peptide.Lactams, Macrocyclic: LACTAMS forming compounds with a ring size of approximately 1-3 dozen atoms.Benzoquinones: Benzene rings which contain two ketone moieties in any position. They can be substituted in any position except at the ketone groups.Molecular Chaperones: A family of cellular proteins that mediate the correct assembly or disassembly of polypeptides and their associated ligands. Although they take part in the assembly process, molecular chaperones are not components of the final structures.Antimicrobial Cationic Peptides: Small cationic peptides that are an important component, in most species, of early innate and induced defenses against invading microbes. In animals they are found on mucosal surfaces, within phagocytic granules, and on the surface of the body. They are also found in insects and plants. Among others, this group includes the DEFENSINS, protegrins, tachyplesins, and thionins. They displace DIVALENT CATIONS from phosphate groups of MEMBRANE LIPIDS leading to disruption of the membrane.Heat-Shock Proteins, Small: A family of low molecular weight heat-shock proteins that can serve as MOLECULAR CHAPERONES.Acclimatization: Adaptation to a new environment or to a change in the old.Peptides, Cyclic: Peptides whose amino and carboxy ends are linked together with a peptide bond forming a circular chain. Some of them are ANTI-INFECTIVE AGENTS. Some of them are biosynthesized non-ribosomally (PEPTIDE BIOSYNTHESIS, NON-RIBOSOMAL).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.Panstrongylus: A genus of cone-nosed bugs of the subfamily TRIATOMINAE. Its species are vectors of TRYPANOSOMA CRUZI.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.Peptide Mapping: Analysis of PEPTIDES that are generated from the digestion or fragmentation of a protein or mixture of PROTEINS, by ELECTROPHORESIS; CHROMATOGRAPHY; or MASS SPECTROMETRY. The resulting peptide fingerprints are analyzed for a variety of purposes including the identification of the proteins in a sample, GENETIC POLYMORPHISMS, patterns of gene expression, and patterns diagnostic for diseases.Oligopeptides: Peptides composed of between two and twelve amino acids.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.Chaperonins: A family of multisubunit protein complexes that form into large cylindrical structures which bind to and encapsulate non-native proteins. Chaperonins utilize the energy of ATP hydrolysis to enhance the efficiency of PROTEIN FOLDING reactions and thereby help proteins reach their functional conformation. The family of chaperonins is split into GROUP I CHAPERONINS, and GROUP II CHAPERONINS, with each group having its own repertoire of protein subunits and subcellular preferences.Electrophoresis, Gel, Two-Dimensional: Electrophoresis in which a second perpendicular electrophoretic transport is performed on the separate components resulting from the first electrophoresis. This technique is usually performed on polyacrylamide gels.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.Kinetics: The rate dynamics in chemical or physical systems.HSC70 Heat-Shock Proteins: A constitutively expressed subfamily of the HSP70 heat-shock proteins. They preferentially bind and release hydrophobic peptides by an ATP-dependent process and are involved in post-translational PROTEIN TRANSLOCATION.Shock, Cardiogenic: Shock resulting from diminution of cardiac output in heart disease.Stress, Physiological: The unfavorable effect of environmental factors (stressors) on the physiological functions of an organism. Prolonged unresolved physiological stress can affect HOMEOSTASIS of the organism, and may lead to damaging or pathological conditions.Cell Line: Established cell cultures that have the potential to propagate indefinitely.

A segment of cold shock protein directs the folding of a combinatorial protein. (1/35)

It has been suggested that protein domains evolved by the non-homologous recombination of building blocks of subdomain size. In earlier work we attempted to recapitulate domain evolution in vitro. We took a polypeptide segment comprising three beta-strands in the monomeric, five-stranded beta-barrel cold shock protein (CspA) of Escherichia coli as a building block. This segment corresponds to a complete exon in homologous eukaryotic proteins and includes residues that nucleate folding in CspA. We recombined this segment at random with fragments of natural proteins and succeeded in generating a range of folded chimaeric proteins. We now present the crystal structure of one such combinatorial protein, 1b11, a 103-residue polypeptide that includes segments from CspA and the S1 domain of the 30S ribosomal subunit of E. coli. The structure reveals a segment-swapped, six-stranded beta-barrel of unique architecture that assembles to a tetramer. Surprisingly, the CspA segment retains its structural identity in 1b11, recapitulating its original fold and deforming the structure of the S1 segment as necessary to complete a barrel. Our work provides structural evidence that (i) random shuffling of nonhomologous polypeptide segments can lead to folded proteins and unique architectures, (ii) many structural features of the segments are retained, and (iii) some segments can act as templates around which the rest of the protein folds.  (+info)

Gene expression regulation by the Curli activator CsgD protein: modulation of cellulose biosynthesis and control of negative determinants for microbial adhesion. (2/35)

Curli fibers, encoded by the csgBAC genes, promote biofilm formation in Escherichia coli and other enterobacteria. Curli production is dependent on the CsgD transcription activator, which also promotes cellulose biosynthesis. In this study, we investigated the effects of CsgD expression from a weak constitutive promoter in the biofilm formation-deficient PHL565 strain of E. coli. We found that despite its function as a transcription activator, the CsgD protein is localized in the cytoplasmic membrane. Constitutive CsgD expression promotes biofilm formation by PHL565 and activates transcription from the csgBAC promoter; however, csgBAC expression remains dependent on temperature and the growth medium. Constitutive expression of the CsgD protein results in altered transcription patterns for at least 24 novel genes, in addition to the previously identified CsgD-dependent genes. The cspA and fecR genes, encoding regulatory proteins responding to cold shock and to iron, respectively, and yoaD, encoding a putative negative regulator of cellulose biosynthesis, were found to be some of the novel CsgD-regulated genes. Consistent with the predicted functional role, increased expression of the yoaD gene negatively affects cell aggregation, while yoaD inactivation results in stimulation of cell aggregation and leads to increased cellulose production. Inactivation of fecR results in significant increases in both cell aggregation and biofilm formation, while the effects of cspA are not as strong in the conditions tested. Our results indicate that CsgD can modulate cellulose biosynthesis through activation of the yoaD gene. In addition, the positive effect of CsgD on biofilm formation might be enhanced by repression of the fecR gene.  (+info)

Control and regulation of the cellular responses to cold shock: the responses in yeast and mammalian systems. (3/35)

Although the cold-shock response has now been studied in a number of different organisms for several decades, it is only in the last few years that we have begun to understand the molecular mechanisms that govern adaptation to cold stress. Notably, all organisms from prokaryotes to plants and higher eukaryotes respond to cold shock in a comparatively similar manner. The general response of cells to cold stress is the elite and rapid overexpression of a small group of proteins, the so-called CSPs (cold-shock proteins). The most well characterized CSP is CspA, the major CSP expressed in Escherichia coli upon temperature downshift. More recently, a number of reports have shown that exposing yeast or mammalian cells to sub-physiological temperatures (<30 or <37 degrees C respectively) invokes a co-ordinated cellular response involving modulation of transcription, translation, metabolism, the cell cycle and the cell cytoskeleton. In the present review, we summarize the regulation and role of cold-shock genes and proteins in the adaptive response upon decreased temperature with particular reference to yeast and in vitro cultured mammalian cells. Finally, we present an integrated model for the co-ordinated responses required to maintain the viability and integrity of mammalian cells upon mild hypothermic cold shock.  (+info)

Global effects of homocysteine on transcription in Escherichia coli: induction of the gene for the major cold-shock protein, CspA. (4/35)

Homocysteine (Hcy) is a thiol-containing amino acid that is considered to be medically important because it is linked to the development of several life-threatening diseases in humans, including cardiovascular disease and stroke. It inhibits the growth of Escherichia coli when supplied in the growth medium. Growth inhibition is believed to arise as a result of partial starvation for isoleucine, which occurs because Hcy perturbs the biosynthesis of this amino acid. This study attempted to further elucidate the inhibitory mode of action of Hcy by examining the impact of exogenously supplied Hcy on the transcriptome. Using gene macroarrays the transcript levels corresponding to 68 genes were found to be reproducibly altered in the presence of 0.5 mM Hcy. Of these genes, the biggest functional groups affected were those involved in translation (25 genes) and in amino acid metabolism (19 genes). Genes involved in protection against oxidative stress were repressed in Hcy-treated cells and this correlated with a decrease in catalase activity. The gene showing the strongest induction by Hcy was cspA, which encodes the major cold-shock protein CspA. RT-PCR and reporter fusion experiments confirmed that cspA was induced by Hcy. Induction of cspA by Hcy was not caused by nutritional upshift, a stimulus known to induce CspA expression, nor was it dependent on the presence of a functional CspA protein. The induction of cspA by Hcy was suppressed when isoleucine was included in the growth medium. These data suggest that the induction of CspA expression in the presence of Hcy occurs because of a limitation for isoleucine. The possibility that Hcy-induced cspA expression is triggered by translational stalling that occurs when the cells are limited for isoleucine is discussed.  (+info)

Cold shock domain proteins and glycine-rich RNA-binding proteins from Arabidopsis thaliana can promote the cold adaptation process in Escherichia coli. (5/35)

Despite the fact that cold shock domain proteins (CSDPs) and glycine-rich RNA-binding proteins (GRPs) have been implicated to play a role during the cold adaptation process, their importance and function in eukaryotes, including plants, are largely unknown. To understand the functional role of plant CSDPs and GRPs in the cold response, two CSDPs (CSDP1 and CSDP2) and three GRPs (GRP2, GRP4 and GRP7) from Arabidopsis thaliana were investigated. Heterologous expression of CSDP1 or GRP7 complemented the cold sensitivity of BX04 mutant Escherichia coli that lack four cold shock proteins (CSPs) and is highly sensitive to cold stress, and resulted in better survival rate than control cells during incubation at low temperature. In contrast, CSDP2 and GRP4 had very little ability. Selective evolution of ligand by exponential enrichment (SELEX) revealed that GRP7 does not recognize specific RNAs but binds preferentially to G-rich RNA sequences. CSDP1 and GRP7 had DNA melting activity, and enhanced RNase activity. In contrast, CSDP2 and GRP4 had no DNA melting activity and did not enhance RNAase activity. Together, these results indicate that CSDPs and GRPs help E.coli grow and survive better during cold shock, and strongly imply that CSDP1 and GRP7 exhibit RNA chaperone activity during the cold adaptation process.  (+info)

Bacterial toxicity of potassium tellurite: unveiling an ancient enigma. (6/35)

Biochemical, genetic, enzymatic and molecular approaches were used to demonstrate, for the first time, that tellurite (TeO(3) (2-)) toxicity in E. coli involves superoxide formation. This radical is derived, at least in part, from enzymatic TeO(3) (2-) reduction. This conclusion is supported by the following observations made in K(2)TeO(3)-treated E. coli BW25113: i) induction of the ibpA gene encoding for the small heat shock protein IbpA, which has been associated with resistance to superoxide, ii) increase of cytoplasmic reactive oxygen species (ROS) as determined with ROS-specific probe 2'7'-dichlorodihydrofluorescein diacetate (H(2)DCFDA), iii) increase of carbonyl content in cellular proteins, iv) increase in the generation of thiobarbituric acid-reactive substances (TBARs), v) inactivation of oxidative stress-sensitive [Fe-S] enzymes such as aconitase, vi) increase of superoxide dismutase (SOD) activity, vii) increase of sodA, sodB and soxS mRNA transcription, and viii) generation of superoxide radical during in vitro enzymatic reduction of potassium tellurite.  (+info)

Role of RNA structure and susceptibility to RNase E in regulation of a cold shock mRNA, cspA mRNA. (7/35)

Degradation of the cspA mRNA in vivo is very rapid at temperatures greater than 30 degrees C and is moderately dependent on RNase E. Investigations in vitro show that degradosomes prepared from normal or cold-shocked cultures cleave the cspA mRNA preferentially at a single site in vitro between two stem-loops approximately 24 residues 3' to the termination codon and approximately 31 residues from the 3' end. The site of cleavage is independent of the temperature and largely independent of the phosphorylation status of the 5' end of cspA mRNA. A 5' stem-loop, potential occlusion of the initiation and termination codons, temperature-dependent translational efficiency, and the position of the RNase E cleavage site can explain the differential stability of the cspA mRNA.  (+info)

Dimorphic aggregation behavior of a fusion polypeptide incorporating a stable protein domain (EGFP) with an amyloidogenic sequence (retroCspA). (8/35)


The cold shock domain (CSD) is a nucleic acid binding domain that is widely conserved from bacteria to higher plants and animals. In Escherichia coli, cold shock proteins (CSPs) are composed solely of a CSD and function as RNA chaperones that destabilize RNA secondary structures. Cellular RNAs tend to be folded into unfavorable structures under low temperature conditions, and RNA chaperones resolve these structures, recovering functionality of the RNAs. CSP functions are associated mainly with cold adaptation, but they are also involved in other biological processes under normal growth conditions. Eukaryotic CSD proteins contain auxiliary domains in addition to the CSD and regulate many biological processes such as development and stress tolerance. In plants, it has been demonstrated that CSD proteins play essential roles in acquiring freezing tolerance. In addition, it has been suggested that some plant CSD proteins regulate embryo development, flowering time and fruit development. In this review, we
RNA can typically fold into several isoenergetic structures, giving place to misfolded and non-functional structures. It is known that proteins can assist in RNA folding by two different mechanisms: binding and stabilizing specific structures, or by what is called RNA chaperone activity (RCA), an activity that accelerates folding through the resolution of misfolded structures or inhibition of their formation. Therefore one goal is to gain insight into RNA chaperone function on an atomic level. We use CspA as a model of RNA chaperone. CspA is the major cold shock protein in E. coli. It is a 70 residues protein that serves to induce adaptation to cold shock conditions (10-15°). Previous studies in our group on CspA dynamics showed that the protein is 1% unfolded at 32°C (M. Tollinger, unpublished results), it has single-stranded nucleic acid binding capacity. It is supposed to act as transcriptional anti-terminator for cold shock genes. We have already determined the solution structure of CspA ...
MON 87460 contains a gene that expresses cold shock protein B (CSPB) from Bacillus subtilis. Expression of this gene confers a yield advantage when yield is limited by water availability. Compositional analyses of MON 87460 and a conventional corn variety with similar background genetics were conduc …
The p-value tells us whether or not a genes expression changes significantly but it is hard to know if that was due to cold shock or any other factor. The p-value of the profile gives us the significance of a particular group of genes, which should give us a better idea of which group of genes responded to cold shock, and get rid of some the possible random genes that were changed. The gene ontology p-value furthers specifies which gene could be affected by cold shock together by grouping the genes with their specific transcription factors. Each p-value allows us to narrow in on genes that are related to each other and helps to identify which genes were changed significantly, specifically due to cold shock ...
CSDE1 antibody [N2C1], Internal (cold shock domain containing E1, RNA-binding) for ICC/IF, IHC-P, WB. Anti-CSDE1 pAb (GTX116218) is tested in Human samples. 100% Ab-Assurance.
Cold shock proteins (Csps) are multifunctional nucleic acid binding proteins used to regulate a wide range of gene expression responses in bacteria. We report here that Csps regulate the production of the pore-forming cytolysin listeriolysin (LLO) and hemolysis phenotypes in Listeria monocytogenes. A triple csp gene deletion mutant incapable of producing any Csps, as well as double csp gene deletion mutants only producing either CspA or CspD, caused less hemolysis and produced lower LLO concentration. On the other hand, another double csp gene deletion mutant that produces CspB retained hemolysis and LLO production levels that are similar to the parental wild-type strain. Transcription analysis showed that in absence of all three csp genes or cspB alone, L. monocytogenes cells have decreased levels of hly gene transcripts, which code for the synthesis of LLO proteins. A comparative examination of mRNA stability showed that hly transcripts were more rapidly degraded in L. monocytogenes triple csp ...
This 20-page report explains how cold shock is a type of hormesis, which is a description of a type of stress that, in the right doses, is enough to shock the body and kick off adaptive processes and response mechanisms that are hardwired into our genes, and, once on, are able to create a resilience that actually exceeds what was needed to counter the initial stimuli. Rhonda discusses how cold exposure increases norepinephrine up to 5-fold in the brain and what the temperature and duration needed to do this are, how norepinephrine has an effect on mood, vigilance, focus, and attention, how cold exposure increases cold shock proteins including one in the brain that repairs damaged synapses and in muscle prevents atrophy, how cold-induced norepinephrine lowers inflammation and pain by decreasing the levels of 3 inflammatory mediators, how chronic cold shock may increase immune cell numbers and particularly a type of immune cell that kills cancer cells, how cold exposure increases metabolic rate, ...
Cold shock of JH642 cells in the absence of an isoleucine supply showed a decrease in viable cell number that corresponds to the decrease in OD. These cultures show an increasing absorption after more than 48 h of cold shock, with a concomitant increase in cell number (data not shown). Repeating cold shock with these cultures (i.e., diluting the cells in fresh medium, growing them at 37°C, and performing a new cold shock experiment) revealed the same growth pattern as seen before with a cold-sensitive phenotype (data not shown). Therefore the occurrence of spontaneous mutation as a putative reason for this phenomenon is not likely. As the decrease in OD and viable cell number after 18 h of cold shock indicate, a large number of cells might lyse, delivering a reasonable amount of free isoleucine and threonine into the medium that is beneficial for viable cells to adapt and restart slow growth. This scenario was corroborated by a fatty acid analysis, where these cell cultures revealed a fatty ...
110125DNAArtificial SequenceSynthetic primer for PCR to amplify of p53 gene 1ttgtttatgg tgtgaggtgt aggag 25225DNAArtificial SequenceSynthetic primer for PCR to amplify of p53 gene 2ctagtttgct aggaggttgg ttggt 25325DNAArtificial SequenceSynthetic primer for PCR to amplify of TP53 gene 3gcagtggctc acgaatccca cactc 25425DNAArtificial SequenceSynthetic primer for PCR to amplify of TP53 gene 4tgagtcaggc ccttctgtct tgaac 25525DNAArtificial SequenceSynthetic primer for PCR to amplify of Bc12 gene 5atggcgcacg ctgggagaac agggt 25625DNAArtificial SequenceSynthetic primer for PCR to amplify of Bc12 gene 6acctacccag cctccgttat cctgg 25725DNAArtificial SequenceSynthetic primer for PCR to amplify of EGFR gene 7ttcctttcat gctctcttcc ccagg 25825DNAArtificial SequenceSynthetic primer for PCR to amplify of EGFR gene 8ggctacggcg gtgtaggaga tgcca 25925DNAArtificial SequenceSynthetic primer for PCR to amplify of CDK9 gene 9cccaggtgtg gccaaacgtg gacaa 251025DNAArtificial SequenceSynthetic primer for PCR to amplify of ...
DNA binding protein A (dbpA) belongs to the Y-box binding protein family, characterized by an 80 amino-acid cold shock domain that imparts DNA-binding activity. It is also known as cold shock domain protein A (CSDA), CSDA1, ZO-1-associated nucleic acid-binding protein (ZONAB), and single-strand DNA-binding protein NF-GMB. DbpA has been reported to bind to the promoter for granulocyte-macrophage colony-stimulating factor (GM-CSF) and act as a repressor of transcription. It also binds to full-length mRNA and small RNAs containing the consensus site UCCAUCA, suggesting a role as a repressor of translation. Mutations in the CSDA gene have been associated with hepatocarcinogenesis.. ...
DNA binding protein A (dbpA) belongs to the Y-box binding protein family, characterized by an 80 amino-acid cold shock domain that imparts DNA-binding activity. It is also known as cold shock domain protein A (CSDA), CSDA1, ZO-1-associated nucleic acid-binding protein (ZONAB), and single-strand DNA-binding protein NF-GMB. DbpA has been reported to bind to the promoter for granulocyte-macrophage colony-stimulating factor (GM-CSF) and act as a repressor of transcription. It also binds to full-length mRNA and small RNAs containing the consensus site UCCAUCA, suggesting a role as a repressor of translation. Mutations in the CSDA gene have been associated with hepatocarcinogenesis.. ...
For 3-minutes, the cryo chamber will cool the surface of your skin by 30-50°F using gasified nitrogen to activate the bodys powerfully healing "cold-shock response". During the session, blood rushes to your core, your body burns 400-800 calories to stay warm and once the sessions is over, the blood returns to the extremities carrying newly released neurotransmitters and "cold-shock" proteins that dramatically lower inflammation, heal injuries, increase collagen levels, boost your mood, accelerate recovery, increase focus and leave you feeling vibrant and full of energy.. ...
Used new algoithm to construct temporal networks of yeasts response to various stresses, including cold shock. For cold shock data, the paper analyzes data from the Gasch, et al. (2000) paper. Supplementary data has cold shock temporal response, but does not show any interactions between transcription factors and targets. (Note: the Gasch et al. paper does not have a true "cold shock" response. They only measure the effect of a temperature shift from 37°C to 25°C. - Kam D. Dahlquist 16:59, 22 September 2008 (EDT)) ...
Dangers of Cold Water Swimming -Cold Shock Response is the physiological response of organisms to sudden cold, in this case humans and cold water.
CircuLex Human CIRP ELISA Kit from MBL. This Kit is used for the quantitative measurement of human CIRP in cell lysate, cell culture supernatants, and other biological media.
The emergence and spread of antimicrobial resistance is the most urgent current threat to human and animal health. An improved understanding of the abundance of antimicrobial resistance genes and genes associated with microbial colonisation and pathogenicity in the animal gut will have a major role in reducing the contribution of animal production to this problem. Here, the influence of diet on the ruminal resistome and abundance of pathogenicity genes was assessed in ruminal digesta samples taken from 50 antibiotic-free beef cattle, comprising four cattle breeds receiving two diets containing different proportions of concentrate. Two hundred and four genes associated with antimicrobial resistance (AMR), colonisation, communication or pathogenicity functions were identified from 4966 metagenomic genes using KEGG identification. Both the diversity and abundance of these genes were higher in concentrate-fed animals. Chloramphenicol and microcin resistance genes were dominant in samples from forage-fed
Amsterdam. This year Amsterdam are hosting the regional conference, so its good to se them represented as a new team as well. They are working on making E. Coli that will grow at temperatures far below normal limits. They also aimed to make coli better at resisting frost. Apparently they have had some success in making the cold resistance work. If you want to read more check our post!. Bilkent_UNAM-Turkey. This team is working on using microalgae for biodegradation. Now this use of microorganisms has been a returning theme for many years, but algae are still somewhat new on the iGEM scene. Bilkent_UNAM are specifically working on degrading TNT. Apparently they didnt get to test their constructs against. Copenhagen. Its good to see a new Danish team in the competition. Copenhagen are working with cytochrome P450 hydroxylases to rid the world of evil. They want to use E. coli expressing two different CYPs to bring death to fungi and environmental estrogens. They seem to have had a bumpy ride ...
Dehydrin, 50 µg. Dehydrins are a family of proteins that become abundant during dessication in seedlings and embryos of cereal crop plants including barley, corn, wheat and rice.
Probable DEAD-box RNA helicase. May work in conjunction with the cold shock proteins to ensure proper initiation of transcription at low and optimal temperatures.
The paliavana parent is P. tenuiflora, the best of the paliavanas. The hybrid does a better job of retaining its foliage than most paliavanas. The sinningia parent is S. conspicua, from which the hybrid acquires the generally white corolla color, the markings and yellow in the throat, and fragrance that can be detected at certain times. The plant has a tuber, an inheritance from its sinningia parent. Paliavana tenuiflora is much more vulnerable to cold than Sinningia conspicua. The hybrid seems to have the latters cold resistance. ...
CircuLex Human CIRP ELISA Kit from MBL. This Kit is used for the quantitative measurement of human CIRP in cell lysate, cell culture supernatants, and other biological media.
Lin28 cold-shock domain complex. Computer model showing the structure of a Lin28 cold-shock domain (purple) complexed with the single-stranded DNA (deoxyribonucleic acid) fragment heptathymidine (yellow). - Stock Image C035/5941
Human CSDA partial ORF ( NP_003642, 241 a.a. - 330 a.a.) recombinant protein with GST-tag at N-terminal. (H00008531-Q01) - Products - Abnova
Cyanobacterial and algal mass development, or blooms, have severe effects on freshwater and marine systems around the world. Many of these phototrophs produce a variety of potent toxins, contribute to oxygen depletion, and affect water quality in several ways. Coexisting antagonists, such as cyanolytic bacteria, hold the potential to suppress, or even terminate, such blooms, yet the nature of this interaction is not well studied. We isolated 31 cyanolytic bacteria affiliated with the genera Pseudomonas, Stenotrophomonas, Acinetobacter, and Delftia from three eutrophic freshwater lakes in Sweden and selected four phylogenetically diverse bacterial strains with strong-to-moderate lytic activity. To characterize their functional responses to the presence of cyanobacteria, we performed RNA sequencing (RNA-Seq) experiments on coculture incubations, with an initial predator-prey ratio of 1: 1. Genes involved in central cellular pathways, stress-related heat or cold shock proteins, and antitoxin genes ...
After the first flush has happened do you need to do anything else like cold shock again or will more flushes just happen? How do you then distinguish between the flushes?
Chronic infections are often attributed to bacterial biofilms. These biofilms are extremely tolerant to antimicrobial treatment due to the presence of dormant persister cells. Whilst a number of persister genes and pathways have been identified, it is likely that others remain. Investigating persistence of S. Typhimurium was therefore undertaken. A csp null mutant of Salmonella enterica sv. Typhimurium, lacking all six cold shock protein (CspA) paralogues was previously constructed (Hutchinson 2005). At 10°C, this strain is unable to divide, but remains viable for several weeks. However it remains capable of growth at 37°C and thus is conditionally dormant. Using this strain, the link between dormancy and persistence was investigated. Treatment of stationary phase planktonic cultures with fluoroquinolones revealed persister cells in SL1344. In contrast the csp null mutant was completely eliminated by treatment at 37°C; this could be prevented by cspC or cspE expression, implicating a role for ...
Comparison of Motility, Acrosome, Viability and ATP of Boar Sperm with or without Cold Shock Resistance in Liquid Semen at 17℃ and 4℃, and Frozen-thawed Semen - Boar;Liquid Semen;Motility;Acrosome;ATP;
Conclusions: Flies reared at constant benign temperatures were more fecund at all acclimationtemperatures. In contrast, flies reared under fluctuating natural or laboratory conditions weremore successful in locating food under cool conditions in the field, while constant cool rearingconditions led to high cold resistance. The fluctuating- and low-temperature rearing conditionsresulted in a similar metabolic profile, while the 24C rearing profile was distinct and showeda lack of plasticity. The effects of developmental acclimation on performance are thereforecomplex and cannot be captured through experimental comparisons of constant environments ...
Read 9 responses to: I have a 8 month old baby and she has had a cold for... Find the best answer on Mamapedia - mom trusted since 2006.
Just wondering if anyone else gets cold while on this diet? I have been sole sourcing for approx 6 weeks and my hands are freezing! This isnt the...
This week on Afropop Worldwide, we bring you Afropops trip to Central America: The Panama Beat. In order to research the show, our producer and resident Latin American traveler Marlon Bishop took a trip to Panama to find out what the tiny country linking North and South America is all about. He brought us back some fantastic records and interviews with artists ranging from reggae star Kafu Banton to cumbia tipica siren Nina Campina. Here you can read some of Marlons personal reflections from the trip. A Trip to Panama I cant remember exactly when I first became restless to go to Panama. In the summer of 2009, Afropop sent me to Puerto Rico to research the roots of reggaeton. I was fascinated to learn that the origin of Latin Americas most popular club music was actually not on that island at all, but in Panama, a country rarely mentioned for its music (unfortunately). The deal was sealed after I heard some tracks from Soundway Records excellent three-disc Panama! compilation of golden-age ...
1. is it nesisary to cold shock your casing after each flush, or just for the first one? 2. how should prints be stored.. i have them wraped up in foil and in a baggie, should i put them in the fridge
Proceeding/Conference:Proceedings of CIRP International Symposium - Advanced Design and Manufacture in the Global Manufacturing Era, August 21-22 ...
Hi, its been years I use nosodes to prevent colds with my little daughter. They do usually work if the cold is caught in the first day or very early. I use ene
Cold and flu can be extremely contagious and are usually more common at certain parts of the year. Learn about cold and flu prevention and treatment.
The enzyme, characterized from the bacterium Escherichia coli, is induced upon cold shock and is involved in the formation of a cold-adapted variant of the outer membrane glycolipid lipid A ...
Colds and Flu - Dos & Donts There are beneficial procedures for treating colds and flu that are easily overlooked. Meanwhile, a lot of commonly
Homologues include a putative cold shock inducible protein and a SecY stabilizing protein. Based on experimental determination ... proposes that its C-terminal α-helical 20 amino acid peptide catalyzes Ca2+ flux both in vivo and in vitro. The Ca2+-leak ... the YccA protein of Escherichia coli and the YetJ protein of Bacillus subtilis. These proteins are about 200-250 residues in ... These proteins are distantly related to the ionotropic glutamate-binding protein of the N-methyl D-aspartate (NMDA) receptor of ...
Though typically associated with heat-induced protein expression, RNA thermometers can also regulate cold-shock proteins. For ... signals the beginning of a protein-coding gene which is then translated to a peptide product by the ribosome. In addition to ... Mega R, Manzoku M, Shinkai A, Nakagawa N, Kuramitsu S, Masui R (August 2010). "Very rapid induction of a cold shock protein by ... January 2010). "The cspA mRNA is a thermosensor that modulates translation of the cold-shock protein CspA". Mol. Cell. 37 (1): ...
... upstream of cold shock proteins in E. coli.[2] Discovery[edit]. Attenuation was first observed by Charles Yanofsky in the trp ... Part of the leader transcript codes for a short polypeptide of 14 amino acids, termed the leader peptide. This peptide contains ... Protein-mediated attenuation[edit]. Protein-RNA interactions may prevent or stabilize the formation of an anti-terminator ... coli protein is tryptophan). If the ribosome attempts to translate this peptide while tryptophan levels in the cell are low, it ...
... proteins are also believed to play a role in the presentation of pieces of proteins (or peptides) on the cell ... Protein Folding in the Cytoplasm and the Heat Shock Response. Cold Spring Harb. Perspect. Biol. doi:10.1101/cshperspect.a004390 ... An example of chaperons are the HSP70 (heat shock protein) chaperones. For example, HSPs help new or misfolded proteins to fold ... Other proteins such as, protein disulfide isomerase and calnexin/calreticulin, have chaperone functions and assist protein ...
In strain LTH681, the stress operon dnaK has been characterized in 1999 as a heat shock protein gene. There is only one gene ( ... Inhibition of Listeria monocytogenes in chicken cold cuts can be obtained by addition of sakacin P and sakacin P-producing ... histidine protein kinase and response regulator that are necessary to activate this promoter upon induction by a peptide ... It is composed of 1884661 nucleotides forming 1879 protein genes and 84 RNA genes. Bredholt, S.; Nesbakken, T.; Holck, A. (2001 ...
Function of heat-shock proteins in immunity is based on their ability to bind not only whole proteins, but also peptides. The ... "Characterization and regulation of cold-induced heat shock protein expression in mouse brown adipose tissue". The American ... Heat-shock proteins as DAMPs[edit]. Extracellular heat-shock proteins can be sensed by our immunity as danger associated ... How heat-shock proteins get into extracellular space[edit]. Heat-shock proteins can be secreted from immune cells or tumour ...
... protein. The protein contains a putative 30- amino-acid signal peptide; removal of the signal sequence gives a predicted ... Toxic shock syndrome: Both Streptococcal and Staphylococcal bacteria can cause this syndrome. Clinical manifestations include ... typically in colder climates.[13] ... Urinary abnormalities include blood and protein found in the ... The carboxy terminal portion of the protein exhibits extensive homology with the carboxy terminus of Staphylococcus aureus ...
... accumulation of mineralization-inhibiting proteins and peptides (such as osteopontin and ASARM peptides) occurs in the ... and individuals who immigrate from warm climates to cold climates, especially women who wear traditional veils or dresses that ... while bone aches are not spontaneous but only revealed by pressure or shocks.[citation needed]It differs from renal ... Noncollagenous matrix proteins, enzymes, and relationship to hypophosphatasia and X-linked hypophosphatemia". Periodontology ...
The protein contains a putative 30- amino-acid signal peptide; removal of the signal sequence gives a predicted molecular ... Toxic shock syndrome: Both Streptococcal and Staphylococcal bacteria can cause this syndrome. Clinical manifestations include ... typically in colder climates. The morbidity and mortality of scarlet fever has declined since the 18th and 19th century when ... These vaccines, which are still in the development phase, expose to the person to proteins present on the surface of the group ...
In this method the cells are briefly shocked with an electric field of 10-20 kV/cm, which is thought to create holes in the ... It has been found that growth of Gram-negative bacteria in 20 mM Mg reduces the number of protein-to-lipopolysaccharide bonds ... It is suggested that exposing the cells to divalent cations in cold condition may also change or weaken the cell surface ... Both genes by themselves produce non-functional peptides, however, when expressed together, as when a plasmid containing lacZ-α ...
Interestingly, a peptide-based JNK inhibitor (AM-111, a retro-inverse D-motif peptide from JIP1, formerly known as XG-102) is ... Both JNK and p38 signaling pathways are responsive to stress stimuli, such as cytokines, ultraviolet irradiation, heat shock, ... response to cold and involved in anti-pathogen responses. In addition, they are also involved in morphogenesis, since MPK4 ... A mitogen-activated protein kinase (MAPK or MAP kinase) is a type of protein kinase that is specific to the amino acids serine ...
Ondetti gained inspiration from his previous work on peptides. Peptides are vital in-vivo components, but peptides are cleaved ... Miguel tried to electroplate a knife using a copper sulfate solution, only to shock himself. Both Ondetti brothers went to a ... He refused, citing "I turned it down, because Deulofeu was an outstanding scientist, but he was very cold in the interaction ... "developing an innovative approach to drug design based on protein structure and using it to create the ACE inhibitors, powerful ...
Recipients who lack this protein develop sensitization to this protein from prior transfusions or previous pregnancies, can ... For example, when individuals run the frozen blood sample directly in their veins this cold blood rapidly reaches the heart, ... The patient may present with symptoms of fever, wheezing, coughing, shortness of breath, and circulatory shock. Urgent ... elevated brain natriuretic peptide (BNP), elevated central venous pressure (CVP), evidence of left heart failure, evidence of ...
Peptides encoded by human lncRNAs have been found in cells and adult tissues. The protein SPAR has been found to be encoded by ... These elements are transcribed as ncRNAs by RNAP III in response to environmental stresses such as heat shock, where they then ... 2004). "The Air noncoding RNA: an imprinted cis-silencing transcript". Cold Spring Harbor Symposia on Quantitative Biology. 69 ... In the broad sense, this mechanism allows the cell to harness RNA-binding proteins, which make up one of the largest classes ...
... is a G protein-coupled receptor that binds to a class of pituitary peptide hormones known as the melanocortins, which include ... nonselective peptide antagonist MC1R has a slightly different function in cold-blooded animals such as fish, amphibians, and ... Shock. 47 (1): 79-85. doi:10.1097/SHK.0000000000000708. PMC 5167637 . PMID 27488084. Maresca V, Flori E, Picardo M (July 2015 ... α-MSH - nonselective peptide full agonist β-MSH - nonselective peptide full agonist γ-MSH - nonselective peptide full agonist ...
2010). "Protein Folding in the Cytoplasm and the Heat Shock Response". Cold Spring Harb Perspect Biology. 2: 1-18. doi:10.1101/ ... This facilitates the correct folding of multi-domain proteins. The newly synthesized peptide chain exits the ribosome into the ... The mitochondrial unfolded protein response detects imbalances in protein stoichiometry of mitochondrial proteins and misfolded ... with the entire protein landscape changing due to loss of other proteins' interactions with the degraded protein. Multiple ...
... heat shock and oxidative stress responses, by activating proteins such as MnSOD and Catalase. Expression of FOXO in the ... Insulin Signalling Insulin and IGF1 are peptide hormones dictating energy functions such as glucose and lipid metabolism. The ... Cold Spring Harbor Perspectives in Biology. 6 (1): a009191. doi:10.1101/cshperspect.a009191. PMC 3941218 . PMID 24384568. Check ... "daf-16 Forkhead box protein O [Caenorhabditis elegans] - Gene - NCBI". Lin, K.; Hsin, H.; Libina, N.; ...
... peptide - peptide 946 - percutaneous ethanol injection - percutaneous transhepatic biliary drainage - percutaneous transhepatic ... fusion protein G-CSF - gabapentin - Gail model - gallium nitrate - gallium scan - gamma irradiation - gamma knife - gamma ray ... cold nodule - Coley's toxins - collagen disease - collagenase - collecting duct - coloanal anastomosis - coloanal pull-through ... anaphylactic shock - anaplastic - anaplastic large cell lymphoma - anaplastic thyroid cancer - anastomosis - anastrozole - ...
The bees violently vibrate their flight muscles in much the same way as they do to heat the hive in cold conditions. This ... Large insects like Mantises are key protein sources for hornet species including Giant hornet to feed their queen and drone ... Fatalities from envenomation are primarily related to anaphylactic shock or cardiac arrest, though rare cases have occurred ... a cytolytic peptide (specifically, a mastoparan) that can damage tissue by stimulating phospholipase action, in addition to its ...
At the end of culturing, the IgG contained in the medium is purified by an affinity-column using Protein A as the adsorbent, ... These diseases include atopic dermatitis, various subtypes of physical urticaria (solar, cold-induced, local heat-induced, or ... although the peptide elements on IgE involved in binding to low affinity IgE receptor (FcεRII) on many cell types are different ... would invariably activate mast cells and basophils and cause anaphylactic shocks and probably deaths among injected persons. ...
Carboxypeptidase cleaves peptide linkages during digestion of proteins. A coordinate covalent bond is formed between the ... Similar alloys with the addition of a small amount of lead can be cold-rolled into sheets. An alloy of 96% zinc and 4% ... Recent research suggests that the topical antimicrobial zinc pyrithione is a potent heat shock response inducer that may impair ... In proteins, zinc ions are often coordinated to the amino acid side chains of aspartic acid, glutamic acid, cysteine and ...
... expressed in mammalian testes and somatic cells form RNA-protein complexes with Piwi proteins. These piRNA complexes (piRCs) ... These RNA elements form one of two possible structures in regions encoding very short peptide sequences that are rich in the ... Comparison of nucleotide sequences and secondary structure models". Cold Spring Harbor Symposia on Quantitative Biology. 31: ... The B2 RNA is a small noncoding RNA polymerase III transcript that represses mRNA transcription in response to heat shock in ...
RvD5 reduced blood levels of bacteria, serum levels of the pro-inflammatory cytokines TNF-α and IL-1β, and a symptom of shock ... However, many resolvins appear to operate at least in part by acting through the following G protein-coupled receptors (GPRs): ... Serhan, C. N.; Chiang, N; Dalli, J; Levy, B. D. (2014). "Lipid mediators in the resolution of inflammation". Cold Spring Harbor ... 1) RvD1 and AT-RvD1 act through the Formyl peptide receptor 2, which is also activated by certain lipoxins and is therefore ...
Shock phase: During this phase, the body can endure changes such as hypovolemia, hypoosmolarity, hyponatremia, hypochloremia, ... Multiple CRH peptides have been identified, and receptors have been identified on multiple areas of the brain, including the ... Cohen S.; Doyle W. J.; Skoner D. P.; Rabin B. S.; Gwaltney Jr J. M. (1997). "Social ties and susceptibility to the common cold ... fat and amino acid/protein concentration in blood. Moreover, they cause lymphocytopenia, eosinopenia, neutrophilia and ...
Disulfide bonds (S-S bonds) between cysteine residues in peptide chains are very important in protein assembly and structure. ... Amorphous or "plastic" sulfur is produced by rapid cooling of molten sulfur-for example, by pouring it into cold water. X-ray ... Molten sulfur is sometimes still used for setting steel bolts into drilled concrete holes where high shock resistance is ... Inorganic sulfur forms a part of iron-sulfur clusters as well as many copper, nickel, and iron proteins. Most pervasive are the ...
Amino acids, the building blocks of proteins, are easily synthesized in plausible prebiotic conditions, as are small peptides ( ... About 4.5 Ga, the nebula began a contraction that may have been triggered by the shock wave from a nearby supernova. A shock ... Most paleoclimatologists think the cold episodes were linked to the formation of the supercontinent Rodinia. Because Rodinia ... Nelson, K.E.; Levy, M. & Miller, S.L. (April 2000). "Peptide nucleic acids rather than RNA may have been the first genetic ...
The balance between potassium and sodium is maintained by ion transporter proteins in the cell membrane.[231] The cell membrane ... All the alkali metals react vigorously or explosively with cold water, producing an aqueous solution of a strongly basic alkali ... Nellis, W. J.; Weir, S. T.; Mitchell, A. C. (1999). "Metallization of fluid hydrogen at 140 GPa (1.4 Mbar) by shock compression ... Solid state crystal structures have been determined for many complexes of alkali metal ions in small peptides, nucleic acid ...
Oneyama C, Nakano H, Sharma SV (March 2002). "UCS15A, a novel small molecule, SH3 domain-mediated protein-protein interaction ... Cold Spring Harbor Symposia on Quantitative Biology. 53 Pt 2 (2): 915-20. doi:10.1101/sqb.1988.053.01.105. PMID 3254788.. ... "Potential role of Gab1 and phospholipase C-gamma in osmotic shock-induced glucose uptake in 3T3-L1 adipocytes". Hormone and ... NUCLEAR MAGNETIC RESONANCE STRUCTURE OF AN SH2 DOMAIN OF PHOSPHOLIPASE C-GAMMA1 COMPLEXED WITH A HIGH AFFINITY BINDING PEPTIDE ...
mRNA and Protein(s) * WP_012289092.1 Peptide Sequence See identical proteins and their annotated locations for WP_012289092.1 ... cold-shock protein. Locus tag. VNG_RS00395. Gene type. protein coding. Organism. Halobacterium salinarum NRC-1 (strain: NRC-1; ... VNG_RS00395 cold-shock protein [ Halobacterium salinarum NRC-1 ] Gene ID: 1447033, updated on 30-Jan-2018 ... General protein information Go to the top of the page Help Names. cold-shock protein. ...
... with subsequent peptide-mapping protein identification. Regarding approximately 600-700 distinct protein spots detected on 2D ... term periods of cold followed by a brief frost treatment were studied in order to disclose proteins responsible for the cold ... Moreover, there have been found several proteins with large increase in accumulation, e.g., 33 kDa oxygen evolving protein of ... The range of changes in protein abundance was generally higher in leaves and chloroplast proteins were frequently affected ...
Owing to the fact that the overexpression of GRPs can confer tolerance to stress (e.g., some are involved in cold acclimation ... Several proteins, including the glycine-rich protein (GRP) superfamily, are involved in cellular stress responses and signaling ... GRPs of class IV [RNA-binding proteins (RBPs)] are involved in alternative splicing or regulation of transcription and stomatal ... those proteins emerge playing a promising role in agriculture through their potential engineering by means of plant genetic ...
Cold Shock Proteins And Peptides. Cellular proteins and peptides that are induced in response to cold stress. They are found in ... Exercise Challenge in a Cold Chamber. The purpose of this study is to compare the exercise-challenge in a cold chamber at 2-4°C ... This study investigated cold chains for farmed oysters raised in t.... Loop-mediated isothermal amplification assay as a point- ... During cold-starvation, PMA qPCR selectively excluded DNAs from heat-killed cells. However, there may be some penetration of ...
Biophysical studies of the development of amyloid fibrils from a peptide fragment of cold shock protein B. Eur. J. Biochem. 267 ... For the native protein, as expected, one cysteine per protein was free, whereas for the full oligomer fraction we obtained 0.2 ... 2001) and by stopped-flow CD for the bovine protein as well as the equine protein (Hamada et al. 1996; Arai et al. 1998; ... a) Elution profiles of the native protein (continuous line) and of the protein heated for 105 min at 67.5°C (20 mg/mL in 10 mM ...
We characterized Cryptococcus neoformans recombinant antiphagocytic protein 1 (rApp1) by SDS-PAGE, gel filtration ... Formation of amyloid fibrils by peptides derived from the bacterial cold shock protein CspB. Protein Sci. 1999;8(6):1350-7. ... App1: an antiphagocytic protein that binds to complement receptors 3 and 2. J Immunol. 2009;182(1):84-91.PubMedGoogle Scholar ... Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods ...
Homologues include a putative cold shock inducible protein and a SecY stabilizing protein. Based on experimental determination ... proposes that its C-terminal α-helical 20 amino acid peptide catalyzes Ca2+ flux both in vivo and in vitro. The Ca2+-leak ... the YccA protein of Escherichia coli and the YetJ protein of Bacillus subtilis. These proteins are about 200-250 residues in ... These proteins are distantly related to the ionotropic glutamate-binding protein of the N-methyl D-aspartate (NMDA) receptor of ...
Cells were washed with ice-cold PBS and analyzed by flow cytometry using a FACScan with CellQuest software (BD Biosciences, ... Heat shock protein-chaperoned peptides but not free peptides introduced in the cytosol are presented efficiently by major ... Heat shock protein-peptide complexes, reconstituted in vitro, elicit peptide-specific cytotoxic T lymphocyte response and tumor ... Tumor-Derived Heat Shock Protein 70 Peptide Complexes Are Cross-Presented by Human Dendritic Cells. Elfriede Noessner, Robert ...
... automated protein sequencer to obtain N-terminal amino acid sequences or were digested with trypsin and the mass of the peptide ... the major cold shock protein of Escherichia coli, in cold shock adaptation. J. Bacteriol. 178:4919-4925. ... enterocolitica to produce major cold shock proteins upon cold shock. ... 1997) A family of cold shock proteins in Bacillus subtilis is essential for cellular growth and for efficient protein synthesis ...
We identify proteins associated with the agent of human granulocytic anaplasmosis, an emerging disease, and the encephalitis- ... Annotation of scaffolds representing ∼57% of the genome, reveals 20,486 protein-coding genes and expansions of gene families ... Expression of heat-shock proteins and subolesin affects stress responses, Anaplasma phagocytophilum infection and questing ... AMP, antimicrobial peptide; CAT, cathepsin; CP, haemlipoglyco-carrier protein; CYP450, cytochrome P450; GR, gustatory receptor ...
Lastly, Hidden Markov Model searches identified three protein family motifs, including cold shock domain proteins and fatty ... Lastly, Hidden Markov Model searches identified three protein family motifs, including cold shock domain proteins and fatty ... Lastly, Hidden Markov Model searches identified three protein family motifs, including cold shock domain proteins and fatty ... Lastly, Hidden Markov Model searches identified three protein family motifs, including cold shock domain proteins and fatty ...
human CSDE1 protein: amino acid sequence in first source; unr gene located close to N-ras locus and may interact with it; ... CSDE1 protein, human; NRU protein, human; cold shock domain containing E1, RNA-binding protein, human; p97 protein (unr), human ... Amino Acids, Peptides, and Proteins*Proteins: 90489*Carrier Proteins: 11456*RNA-Binding Proteins: 969*human CSDE1 protein ... p97-unr protein, human; unr protein, human; upstream-of-ras protein, human ...
Even the common cold got its name because it is common in cold weather and rare in the summer. Vitamin D blood levels are at ... called antimicrobial peptides. The 200 known antimicrobial peptides directly and rapidly destroy the cell walls of bacteria, ... the steroid hormone under question increases the bodys production of a remarkable class of proteins, ... The doctors are shocked at my progress. I settled my vaccine case this year with the courts conceding that all of my damage was ...
CSP_CDS; Cold-Shock Protein (CSP) contains an S1-like cold-shock domain (CSD) that is found in eukaryotes, prokaryotes, and ... this study shows that innate immunity activation by muramyl peptides is mediated via an interaction between YB1 and NOD2 Title ... CSPs include the major cold-shock proteins CspA and CspB in bacteria and the eukaryotic gene regulatory factor Y-box protein ... Inflammatory cell infiltration and resolution of kidney inflammation is orchestrated by the cold-shock protein Y-box binding ...
... cells were grown to an OD600 of 1.2 and then cold-shocked and induced with 0.4 mM IPTG for 2 hours before harvesting. Protein ... The peptide bond, the defining feature of proteins, governs peptide chemistry by abolishing nucleophilicity of the nitrogen. ... C in ice-cold water bath (cold shock) before induction with 0.2 mM isopropyl-β-D-thiogalactopyranoside (IPTG) for 20 hours. For ... that are capable of disrupting protein-protein interactions.. Omphalotin A is a fungal peptide macrocycle comprising of 12 ...
... were found to include many RNA binding proteins. To assess the possibility that some of the many cold shock domain proteins ... which in turn was used to classify the different phosphorylated peptides as potential kinase targets. Predicted peptides of ... Pour évaluer la possibilité que quelques-unes des multiples protéines à domaine Cold Shock identifiées dans le transcriptome ... à domaine Cold Shock. Chez L. polyedrum, plusieurs gènes sont répétés en tandem. Un alignement des séquences obtenues par RNA- ...
The cytosolic 70-kDa heat shock proteins (Hsp70s) Ssa and Ssb of. The cytosolic 70-kDa heat shock proteins (Hsp70s) Ssa and Ssb ... For each 40-μl ATPase assay the following concentrations of each peptide unfolded protein or DnaJ-homologue were added: A5 (15 ... The fusion BAA rescues the cold-sensitive phenotype of a disruption strain. Here we demonstrate that this fusion BAA has ... Categories Motor ProteinsTags AEE788, RYBP Influenza B pathogen is a major causative agent of respiratory disease. Influenza B ...
3371). ProS2 is about 23 kDa of a tandem-dimer from the N-terminal domain of Protein S, a soluble protein derived from ... Anti-Protein S monoclonal antibody is used to detect ProS2-fused protein expressed by using pCold ProS2 DNA (Cat. # ... Anti-Protein S Monoclonal Antibody can be used for detection of ProS2-fused proteins expressed from the cold shock expression ... 3371). ProS2 is an approximately 23 kDa soluble tandem-dimer peptide tag derived from the N-terminal domain of Protein S, a ...
... incorporation into proteins and peptides and serving as a primer for branched-chain fatty acids of the anteiso-branching type ( ... the cold shock proteins and the cold acclimatization proteins, respectively, with the cold shock proteins thought to play a ... 1997) Differentiation between cold shock proteins and cold acclimation proteins in a mesophilic gram-positive bacterium, ... subtilis to survive cold shock from 37 to 15°C. Cold shock experiments with strain JH642 revealed a cold-protective function ...
The supernatant, which was the osmotic shock fraction, was recovered and combined with the periplasmic fraction. The mixture ... The harvested cells were resuspended in 1 ml of ice-cold periplasmic extraction buffer I (20% (w/v) sucrose, 100 mM Tris-HCl, ... Several signal peptides of outer membrane proteins (from native and other species) that are transported by the general ... Meanwhile, it is necessary to determine the effects of different signal peptides on a given protein (as well as their mutual ...
Some Characteristics of the Bacteriocin and Cold Shock Protein of the Strain Lactobacillus Plantarum Ul485 Isolated from Chao ... Peptides. 2009;30(8):1562-74. *Barria C, Malecki M, Arraiano CM. Bacterial adaptation to cold. Microbiology. 2013;159(12):2437- ... The gene encoded for cold shock protein (Csp) in the strain was cloned and then the protein was identified as CspC. In addition ... After a rapid temperature downshift, cold shock proteins regulate the adaptation of bacteria to cold stress [6]. ...
Peptides. Proteins. Steroids Powder. GHRP-2. IGF-1 LR3. 17a-Methyl-1-Testosterone. ... Its chemically similar to the ephedrine and pseudoephedrine found in many over-the-counter cold/allergy medications and weight ... 3. Synephrine used in the treatment of bronchial asthma clinical shock and hypotension collapse and orthostatic. hypotension ... peptides products, IGF-1 LR3, and steroids and SARMs products, EGF, VEGF etc., in China. All the managers and engineers are ...
Cold Shock domain. 63. X. 17983. C-CaM/PEP-19 complex. 63. X. ... BMRB Protein/Peptide T1 Entries. listed by number of T1 values ... A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules Member of ... Protein. DNA. RNA. 5569. protein GB1. 1680. X. 5996. Major Urinary Protein-I. 979. X. ...
Cold Shock domain. 28. X. 16482. LRP-1. 28. X. 16218. apoMb(1-119) fragment. 23. X. ... BMRB Protein/Peptide Heteronuclear NOE Entries. listed by number of heteronuclear NOE values in descending order. Number of ... A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules Member of ... Protein. DNA. RNA. 5569. protein GB1. 1680. X. 5996. Major Urinary Protein-I. 979. X. ...
2015) used comparative proteomics to study V. metschnikovii exposed to cold stress, while also applying a novel proteomics ... cold shock proteins, elongation factors, chaperone proteins, ribosomal proteins, outer membrane proteins, and some proteins ... The investigators harvested the cultures and separated the resulting peptide solutions using an EASY-nLC 100 liquid ... cold-stressed cells had greater amounts of cold shock and ribosomal proteins, and decreased proteins involved in energy ...
  • Neither the number nor proportion of proteins in various categories differed significantly, with the exception of proteins categorized by Gene Ontology in pigmentation, biological regulation, transcription regulator activity and transporter activity. (
  • Gene ontology and KEGG pathway analyses revealed the functions and locations of the identified proteins. (
  • Human tumor-derived HSP70 peptide complexes (HSP70-PC) thus have the immunogenic potential to instruct DCs to cross-present endogenously expressed, nonmutated, and tumor antigenic peptides that are shared among tumors of the melanocytic lineage for T cell recognition. (
  • T cell stimulation by HSP70-instructed DCs is dependent on the Ag bound to HSP70 in that only DCs incubated with HSP70-PC purified from tyrosinase-positive (HSP70-PC/tyr + ) but not from tyrosinase-negative (HSP70-PC/tyr − ) melanoma cells resulted in the specific activation of the HLA-A*0201-restricted tyrosinase peptide-specific cytotoxic T cell clone. (
  • HSP70-PC-mediated T cell stimulation is very efficient, delivering the tyrosinase peptide at concentrations as low as 30 ng/ml of HSP70-PC for T cell recognition. (
  • Among them, based on protein expression levels, the HSP70 family consists of the constitutively expressed HSP (HSC70) and the heat-inducible HSP (HSP70) 70-kDa proteins. (
  • As shown in Table ?Table2 2 Ssb was not stimulated by CMLA or any of the peptides tested which are clearly capable of stimulating one or more other Hsp70 subfamily users. (
  • Cer1p/Lhs1p/Ssi1p is a novel Hsp70-related protein that is important for the translocation of a subset of proteins into the yeast Saccharomyces cerevisiae endoplasmic reticulum. (
  • Cer1p has very limited amino acid identity to the hsp70 chaperone family in the N-terminal ATPase domain but lacks homology to the highly conserved hsp70 peptide binding domain. (
  • Cer1p peptide binding and oligomerization could be disrupted by addition of ATP, confirming that Cer1p possesses a functional ATP binding site, much like Kar2p and other members of the hsp70 family. (
  • Since Kar2p is a member of the highly conserved hsp70 family, it is believed to chaperone protein folding in a manner similar to that used by other family members, although no study of this mechanism has been published. (
  • The mechanism of hsp70-dependent protein folding has been best studied by using the bacterial hsp70, DnaK. (
  • The J domain of HSP40 heat shock proteins interacts with HSP70 HEAT-SHOCK PROTEINS. (
  • HSP40 heat-shock proteins play a role in regulating the ADENOSINE TRIPHOSPHATASES activity of HSP70 heat-shock proteins. (
  • J-Z arrays can be found in a group of (hypothetical) proteins in plants, which may share some functions, presumably to recruit specific Hsp70 partners as co-chaperones. (
  • Whereas information on the involvement of blood cells and of proteolytic cascades in Drosophila immunity is still fragmentary, much has been learned in recent years about the structure and regulated expression of the inducible antimicrobial peptides, and we will restrict our analysis here to this facet of the host defense ( 3 ). (
  • In addition to this systemic response, Drosophila also produces antimicrobial peptides locally, in barrier epithelia ( 4 ). (
  • Since the discovery of inducible antimicrobial peptides in the moth Hyalophora cecropia by Boman and associates in 1981 ( 5 ), 400 peptides have been reported to participate in innate immunity, not only in insects but in all multicellular organisms that were investigated, including humans and plants. (
  • Regarding their multifaceted effects, antimicrobial peptides (AMPs), a natural host defense peptide, are one of the more attractive agents for the treatment of these issues, which are not only capable combatting both drug-sensitive and drug-resistant microbial pathogens but also exhibit antiviral and anticancer activities. (
  • 1 (2015) used comparative proteomics to study V. metschnikovii exposed to cold stress. (
  • It significantly boosted the number of proteins analyzable per hour and has now evolved into a proteomics analysis workhorse for many laboratories. (
  • Mass spectrometry (MS)-based 1 proteomics aims at the comprehensive analysis of proteins present in a biological sample ( 1 ), and the field has expanded in many surprising directions ( 2 ). (
  • If we further consider all the peptides produced in bottom-up proteomics experiments, this hurdle is compounded, as ideally many hundreds of thousands of analytes should be characterized in order for the proteins giving rise to them to be fully reconstructed ( 6 ). (
  • Antibodies are used in proteomics both as imaging reagents for the analysis of tissue specificity ( 1 ) and subcellular localization ( 2 ) and as capturing agents for targeted proteomics ( 3 ), in particular for the enrichment of peptides for immunoaffinity methods such as Stable Isotope Standards and Capture by Anti-peptide Antibodies ( 4 ). (
  • Knowledge about the binding site (epitope) of an antibody toward a target protein is thus important for gaining basic insights into antibody specificity and sensitivity and facilitating the identification and design of antigens to be used for reagents in proteomics, as well as for the generation of therapeutic antibodies and vaccines ( 1 , 6 ). (
  • As a preliminary step in making this assessment, we wished to provide proof of principle by performing protein expression proteomics and 16S rRNA sequencing analyses and using bioinformatics analysis to identify major protein functions and pathways. (
  • 2D-DIGE quantitative proteomics comparing the soluble proteomes of sensitive and HePC resistant L. donovani lines identified a protein of interest tentatively involved in drug resistance. (
  • Comparative genome-wide analysis with other fish genomes shows that mitochondrial proteins and hemoglobin evolved rapidly. (
  • Our data and analysis suggest that evolutionary strategies in efficient aerobic cellular respiration are controlled by hemoglobin and mitochondrial proteins, which may be important for the adaptation of Antarctic fish to their environment. (
  • Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition," Cell 102:33-42 (2000). (
  • We show that endogenous mouse SIRT3 is a soluble mitochondrial protein. (
  • SIRT3-deficient animals exhibit striking mitochondrial protein hyperacetylation, suggesting that SIRT3 is a major mitochondrial deacetylase. (
  • Overall, our results extend the recent finding of lysine acetylation of mitochondrial proteins and demonstrate that SIRT3 has evolved to control reversible lysine acetylation in this organelle. (
  • Exposure to the HFD led to hyperacetylation of proteins involved in gluconeogenesis, mitochondrial oxidative metabolism, methionine metabolism, liver injury and the ER (endoplasmic reticulum) stress response. (
  • Livers of mice fed on the HFD had reduced SIRT3 activity, a 3-fold decrease in hepatic NAD + levels and increased mitochondrial protein oxidation. (
  • Our results suggest that SIRT3 is an integral regulator of mitochondrial function and its depletion results in hyperacetylation of critical mitochondrial proteins that protect against hepatic lipotoxicity under conditions of nutrient excess. (
  • 3 ] reported that acetylation of up to 70 mitochondrial proteins in liver changed by at least 2.5-fold in response to caloric restriction, suggesting the importance of extranuclear acetylation in events influencing metabolic fuel utilization. (
  • Assignment of Homology to Genome Sequences using a Library of Hidden Markov Models that Represent all Proteins of Known Structure. (
  • Despite their adaptations to the cold, genome-wide studies have not yet been performed on these fish due to the lack of a sequenced genome. (
  • Here we discuss the sequencing and analysis of the genome of the Antarctic bullhead notothen, N. coriiceps , and report transcriptome analysis from RNA-seq experiments conducted to explore temperature challenges involved in cold-adapted evolution. (
  • Thus, over 55% of all proteins in the genome remain functionally uncharacterized. (
  • Genome sequences, proteomic, and transcriptomic studies suggest various adaptive features to maintain adequate translation and proper protein folding under cold conditions. (
  • E. coli genome does not appear to encode for any protein that has significant homology to OsGR-RBP4 protein. (
  • C/I)(F/Y)(V/I)(G/K)(G/N)L]. Genome sequencing projects have revealed that RRM containing proteins are abundantly present in varied life forms including viruses, prokaryotes as well as eukaryotes. (
  • Inverse PCR was used to amplify major cold shock protein (MCSP) gene families from a diverse range of bacteria, including the psychrotolerant Yersinia enterocolitica , which was found to have two almost identical MCSP coding regions ( cspA1 and cspA2 ) located approximately 300 bp apart. (
  • In addition, cold shock protein (Csp) in the strain and the survival of the bacteria with temperature downshift after freezing were primarily studied. (
  • Many publications show the functions of cold shock proteins (Csp) in the adaptation process of bacteria to new environmental conditions, especially in temperature downshift [ 5 ]. (
  • After a rapid temperature downshift, cold shock proteins regulate the adaptation of bacteria to cold stress [ 6 ]. (
  • Cold stress can enhance the virulence of some bacteria. (
  • Further quantitative real-time reverse transcription polymerase chain reaction (qRT-PCR) analysis identified and quantified 2,066 proteins with an overlap of 1,743 proteins between the control and cold-stressed bacteria. (
  • In the cold challenging environment of the permafrost, bacteria have found a way to survive and grow for thousands to millions of years. (
  • Namely, the inevitable selection of bacteria occurs in each artificial cold environment and the successive changes in microbiota occur according to changes in environmental factors. (
  • Using sequence profile searches we identify a novel domain in these proteins that is widely conserved across eukaryotes and bacteria. (
  • Both bacteria and eukaryotes encode a conserved family of proteins that combines this predicted RNA-binding domain with a previously uncharacterized domain (DUF88). (
  • Protein post-translational modifications in bacteria. (
  • Conserved from bacteria to humans, the sirtuin family of NAD + -dependent protein deacetylase/mono-ADP-ribosyltransferase enzymes controls a variety of cellular processes such as aging, metabolism, and gene silencing ( 18 , 24 ). (
  • More specifically, the invention relates to the vaccination of primates, preferably humans, with protein complexes, such as a purified FimH polypeptides, a purified FimC-FimH (FimCH) polypeptide complex, or immunogenic fragments thereof, to stimulate protective immunity in the recipient against infection by pathogenic bacteria, including all types of Enterobacteriaceae, preferably E. coli to produce specific immunoglobin molecules in the serum and urine or mucosal secretions of the subject. (
  • identified 685 TMBIM proteins in 171 organisms from Archaea, Bacteria, and Eukarya, and provided a phylogenetic overview of the whole TMBIM superfamily. (
  • Csp(s) are a family of proteins with molecular weights around 7 kDa and share a high degree of similarity in their sequences. (
  • Initial work showed that when an exponential-phase culture of E. coli is shifted from 37 to 10°C, a novel set of at least 13 proteins is induced ( 24 ). (
  • In contrast to the relatively minor level of induction (2- to 10-fold) observed for most cold shock proteins during a temperature downshift in E. coli , the induction of a novel protein (initially designated as F10.6) was found to be considerably higher ( 24 ). (
  • This product does not cross-react with proteins derived from E. coli or the TF (Trigger Factor) tag. (
  • PelB and five native E. coli signal peptides, as fusion partners produced more soluble and functional recombinant lipBJ10 than non-fusion expression. (
  • Recombinant lipBJ10, fused to these six diverse signal peptides, was secreted into the periplasm in E. coli . (
  • the other four E. coli signal peptides, to some extent, led to low activity and insoluble inclusion bodies. (
  • Using a smaller PrS-tag, consisting of a single N-terminal domain of protein S, triple resonance experiments were performed, and most of the backbone 1 H, 15 N and 13 C resonance assignments for full-length E. coli RbfA were determined. (
  • RNA binding and chaperone activity of the E. coli cold-shock protein CspA. (
  • This is the YbhL protein of E. coli . (
  • Most of the more closely related homologues of the E. coli SAD protein are of 200-250 aas. (
  • E. coli M15 cells transformed with full-length rice glycine-rich RNA binding protein4 (OsGR-RBP4), truncated rice glycine-rich RNA binding protein4 (OsGR-RBP4ΔC) and rice FK506 binding protein (OsFKBP20) were analyzed for growth profiles using both broth and solid media. (
  • Expression of OsGR-RBP4 and OsGR-RBP4ΔC proteins caused specific, inhibitory effect on growth of recombinant M15 E. coli cells. (
  • Expression of eukaryotic, stress-associated OsGR-RBP4 protein in prokaryotic E. coli M15 cells proves injurious to the growth of the bacterial cells. (
  • This study is dedicated in memory of Ferruccio Ritossa (1936-2014), a great sculptor of biology who discovered the heat-shock response. (
  • Representative adaptations to this harsh environment include a constitutive heat shock response and the evolution of an antifreeze protein in the blood. (
  • Loss of the phosphorylation-dependent sumoylation motif in heat shock factor 1 suggests that the heat shock response evolved into a simple and rapid phosphorylation-independent regulatory mechanism. (
  • Rapidly evolved hemoglobin and the induction of a heat shock response in the blood may support the efficient supply of oxygen to cold-adapted mitochondria. (
  • This paper proposes that the rapid decrease in quantity of most normal proteins occurring in the heat-shock response would have provided a sufficient selective force for the margin of safety to have evolved. (
  • The range of changes in protein abundance was generally higher in leaves and chloroplast proteins were frequently affected which suggests a priority to protect photosynthetic apparatus. (
  • This biochemical analysis is usually of particular interest because it suggests that it is not the B-like activity of the Ssb ATPase domain name that confers rescue of the cold-sensitive phenotype. (
  • The frequent detection of members of above-mentioned genera in artificial cold environments suggests that the important factors that define the existence of these genera in cold artificial environments are i) chances of invasion of such cold environments from ambient environments, ii) chances of invasion through their own basic components, iii) ability to rapidly propagate at low temperature and iv) presence or absence of oxygen. (
  • This result suggests that an interaction with the mature portion of the protein also is important for the translocation role of Cer1p. (
  • The high degree of conservation of the binding interface in sequences of other CSP and the related eukaryotic Y-box proteins suggests, that these proteins do not only have a common ancestor but also share a common mode of ligand binding and display similar binding preferences. (
  • Le transcriptome a aussi été utilisé pour définir le spectre des kinases présentes chez L. polyedrum, qui a ensuite été utilisé pour classifier les différents peptides phosphorylés qui sont potentiellement les cibles de ces kinases. (
  • Bacterial CaTA (BI-1) domains are found in 'fusion' proteins of histidine sensor kinases, diguanylate cyclases and proteins with ABC2-like P-loop ATPase domains. (
  • Unlike Sec63p, Scj1p possesses all the domains thought necessary to function as a DnaJ-like chaperone in protein folding ( 42 ). (
  • In addition to numerous components in immune responses, chaperone proteins are also detected in the extracellular fluids and have been implicated in autoimmune and inflammatory diseases acting as pro- and anti-inflammatory factors. (
  • Therefore, chaperone proteins that assist RNA in adopting their functionally active states are abundant in all living organisms. (
  • An important feature of RNA chaperone proteins is that they do not require an external energy source to perform their activity, and that they interact transiently and non-specifically with their RNA targets. (
  • So far, little is known about the mechanistic details of the RNA chaperone activity of these proteins. (
  • Kwon HY, Park SS, Zia MF, Rhee DK (2016) Protein Expression via the Molecular Chaperone ClpL. (
  • Unlike the DnaK system, which requires an additional co-chaperone system to reinstate the natural conformation of denatured target proteins, pneumococcal ClpL is able to disaggregate denatured proteins independently, without requiring a co-chaperone system. (
  • Accordingly, ClpL could be a useful chaperone system to solubilize foreign proteins during protein overexpression. (
  • Activation of the pathway results in the expression of chaperone protein. (
  • MCSPs are extremely widespread in eubacteria (reference 8 and this study) and belong to the most conserved group of nucleic acid-binding proteins yet defined in nature: the cold shock domain (CSD) proteins ( 40 ). (
  • These small proteins (65 - 70 amino acids) bind single- stranded nucleic acids with micromolar to nanomolar KD values. (
  • This theory proposes that RNA was once the sole nucleic acid present in cells, and was replaced by the current DNA → RNA → protein system. (
  • Nucleic acid sequences encoding such proteins and assays employing same are also disclosed. (
  • SH2 Domain-Containing Protein Tyrosine Phosphatases" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (
  • A subcategory of protein tyrosine phosphatases that contain SH2 type SRC HOMOLOGY DOMAINS. (
  • Below are the most recent publications written about "SH2 Domain-Containing Protein Tyrosine Phosphatases" by people in Profiles. (
  • Rottlerin competes with the PAPS co-factor in sulfotransferases, opening the door for the discovery and optimisation of other kinase inhibitors that inhibit these classes of enzyme, including protein tyrosine sulfotransferases (TPSTs). (
  • Using liver biopsies collected during the early phases of organ procurement and transplantation, we aimed at characterizing the global patterns of tyrosine phosphorylation during hepatic I/R. A proteomic approach, based on the purification of tyrosine phosphorylated proteins followed by their identification using mass spectrometry, allowed us to identify Nck-1, a SH 2 /SH 3 adaptor, as a potential regulator of I/R injury. (
  • After affinity-based enrichment of tyrosine phosphorylated proteins using specific anti-PY antibodies, phosphorylation analysis by mass spectrometry is generally accomplished in a two-step process. (
  • Protein Tyrosine Phosphatases, Non-Receptor" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (
  • A subcategory of protein tyrosine phosphatases that occur in the CYTOPLASM. (
  • Below are the most recent publications written about "Protein Tyrosine Phosphatases, Non-Receptor" by people in Profiles. (
  • This study was performed to compare and optimize signal peptides for efficient secretion of thermostable lipase lipBJ10 from Pseudomonas fluorescens BJ-10. (
  • We recently described active secretion of a family member, denoted Y-box (YB) protein-1. (
  • However it is also possible that none of the peptides or DnaJs used in these assays interact with Ssb. (
  • Knowledge about an antibody's linear epitopes is also useful in, for instance, developing assays involving the capture of peptides obtained from trypsin cleavage of samples prior to mass spectrometry analysis. (
  • In general, the feasibility of this approach largely depends on the secretory pathway of signal peptide and the type of target protein to be secreted. (
  • Therefore, DsbA is the optimal signal peptide partner to fuse with lipBJ10 to efficiently produce soluble and functional protein. (
  • Proteins of interest are proteolytically digested, usually with trypsin, and the resulting peptides are analyzed to determine those which are phosphorylated. (
  • In one of the first studies of isolated intermediates in protein aggregation, we have used circular dichroism and fluorescence spectroscopy to characterize metastable oligomers that are formed in the early steps of β-lactoglobulin heat aggregation. (
  • We characterized Cryptococcus neoformans recombinant antiphagocytic protein 1 (rApp1) by SDS-PAGE, gel filtration chromatography, circular dichroism, and fluorescence spectroscopy. (
  • Isotope-Filtered 2D Hohaha Spectroscopy of a Peptide-Protein Complex Using Heteronuclear Hartmann-Hahn Dephasing. (
  • Title: Muramyl peptides activate innate immunity conjointly via YB1 and NOD2. (
  • Negative control of BAK1 by protein phosphatase 2A during plant innate immunity. (
  • The structure of OphA reveals a complex catenane-like arrangement in which the peptide substrate is clamped with its amide nitrogen aligned for nucleophilic attack on the methyl group of SAM. (
  • Nanoscale liquid chromatography coupled online to mass spectrometry is the current technique of choice for the analysis of complex peptide mixtures. (
  • In wild-type yeast under reducing conditions, pro-CPY can be found in a complex with Cer1p, while partially purified Cer1p is able to bind directly to peptides. (
  • Irrespective of their asymmetrical partitioning, the nuage complex contains several proteins that are conserved throughout animal evolution. (
  • Cryoconite holes on glacier surfaces represent another permanently cold biotope hosting complex microbial communities [ 11 , 12 ]. (
  • Mechanisms of RALF peptide perception by a heterotypic receptor complex. (
  • Promotion of osteoblast proliferation on complex coacervation-based hyaluronic acid and recombinant mussel adhesive protein coatings on titanium. (
  • RATIONALE: Vaccines made from a person's tumor cells, such as gp96 heat shock protein-peptide complex, may help the body build an effective immune response to kill tumor cells. (
  • Resonance Assignment of Methionine Methyl-Groups and Chi(3) Angular Information From Long-Range Proton-Carbon and Carbon- Carbon J-Correlation in a Calmodulin Peptide Complex. (
  • For metaproteomics analysis, peptides were generated by using the Fasp method and subsequently fractionated by strong anion exchanges. (
  • To circumvent the casparian strip (indicated as red band), it has to enter the cytosol of the endodermal cells via channel proteins (shown in blue) and subsequently be exported into the apoplast via Ca 2+ -ATPases or Ca 2+ /H + antiporters (shown in orange) ( Clarkson, 1993 ). (
  • Subsequently, peptides are further analyzed by tandem mass spectrometry (MS/MS), i) to identify the corresponding proteins and ii) to determine the precise location of the phosphorylation site(s). (
  • In the first stages of the secretory pathway, proteins translocate into and fold in the endoplasmic reticulum (ER). (
  • 9,10 identified a unique 16.6-kD secretory protein that was not detectable in the healthy gland but appeared 6 h after induction of experimental pancreatitis, reaching peak values after 48 h. 11 Therefore, the protein was called pancreatitis-associated protein (PAP). (
  • Here we demonstrate the fabrication of a fusion protein comprising of elastin-like peptides and KGF. (
  • This fusion protein retains the performance characteristics of KGF and elastin as evidenced by its enhancement of keratinocyte and fibroblast proliferation. (
  • This includes scaffolds of collagen and solubilized elastin ( 17 ), dermal substitutes coated with 3% α-elastin ( 6 , 18 ), and alginate wound dressings linked with hybrid peptides of elastin ( 19 ). (
  • Relationship of serum elastin peptide level to single breath transfer factor for carbon monoxide in French coal miners. (
  • While chemical methylation of an amide bond uses a strong base to generate the imidate, OphA, the precursor protein of the fungal peptide macrocycle omphalotin A, self-hypermethylates amides at pH 7 using S -adenosyl methionine (SAM) as cofactor. (
  • Lin, Tsan-Piao 2013-04-28 00:00:00 AP2/ERF proteins play crucial roles in plant growth and development and in responses to biotic and abiotic stresses. (
  • Protein and nitrogen metabolic processes have been influenced by low temperature to a similar extent in both tissues while catabolism, carbohydrate metabolism and proteins involved in stress response have been more affected in crowns than in leaves. (
  • Although the participation of GRPs in plant stress response has been indicated in numerous model and non-model plant species, relatively little is known about the key physiological processes and molecular mechanisms in which those proteins are engaged. (
  • Owing to the fact that the overexpression of GRPs can confer tolerance to stress (e.g., some are involved in cold acclimation and may improve growth at low temperatures), these proteins could play a promising role in agriculture through plant genetic engineering. (
  • BI-1 is an ER-localized protein that protects against apoptosis and ER stress. (
  • Temperature shifts are easy to simulate in the laboratory, and the physiological and molecular response to cold stress gained our interest ( 15 ). (
  • It is generally accepted that the cold stress response consists of two phases: an immediate, transient shock response and the subsequent delayed acclimatization response. (
  • 2015) " Proteomic analysis of Vibrio metschnikovii under cold stress using a quadrupole Orbitrap mass spectrometer ," Research in Microbiology, 166(8) (pp. 618-625). (
  • Transcriptome analysis of thermal stress responses find alternative response mechanisms for evolution strategies in a cold environment. (
  • The stress response to heat-shock was originally described in the early '60s by the Italian researcher Ferruccio Ritossa [ 4 ]. (
  • Stress management is accompanied by changes in gene expression which, in turn, modify the collection of metabolites and proteins that are present. (
  • Large increases in Mal d 1-like protein and Mal d 1.03G of 2.70- and 5.98-fold, respectively, were also consistent with reports of this type of protein being induced by stress and disease. (
  • Many of the proteins that were not altered after wounding were also associated with stress response, including others from the Mal d 1 group. (
  • Heat shock proteins and other proteins normally associated with stress were also unchanged, but these are normally associated with cold shock. (
  • Activity-Regulated Cytoskeleton-Associated Protein (Arc/Arg3.1) is Transiently Expressed after Heat Shock Stress and Suppresses Heat Shock Factor 1. (
  • Heat shock proteins are induced by activation of heat shock factor 1 (HSF1) in response to heat shock and protect against heat stress. (
  • 6 ] further reported that GR-RBP2, in Arabidopsis has a positive impact on seed germination and seedling growth of plants under cold stress conditions. (
  • Regarding approximately 600-700 distinct protein spots detected on 2D gels, there has been found at least a two-fold change after exposure to low temperatures in about 10% of proteins in leaves and 13% of proteins in crowns. (
  • The switch to a fatty acid profile dominated by anteiso-C 15:0 and C 17:0 at low temperatures and the cold-sensitive phenotype of isoleucine-deficient strains in the absence of isoleucine focused our attention on the critical role of anteiso-branched fatty acids in the growth of B. subtilis in the cold. (
  • However, little research has investigated the molecular response of V. metschnikovii during adaptation and growth under cold temperatures that allow it to thrive and therefore risk food safety. (
  • The fusion protein self-assembled into nanoparticles at physiological temperatures. (
  • Coping with our cold planet" [ 1 ], the title of this recent review unambiguously stresses a frequently overlooked aspect: the Earth's biosphere is predominantly cold and permanently exposed to temperatures below 5°C. Such low mean temperature mainly arises from the fact that 71% of the Earth's surface is covered by oceans that have a constant temperature of 2-4°C below 1000 m depth, irrespective of the latitude. (
  • Psychrophiles thrive in permanently cold environments (in thermal equilibrium with the medium) and even at subzero temperatures in supercooled liquid water. (
  • Although microglial reaction to heat shock is considered to be protective, heat shock is still a potential hazard caused by high temperatures. (
  • DnaK, like other hsp70s, possesses the ability to bind short hydrophobic peptides and hydrolyze ATP ( 11 , 33 ). (
  • One of these proteins, TEGT or the Bax Inhibitor-1 (TC# 1.A.14.1.1), has a C-terminal domain that forms a Ca2+-permeable channel. (
  • Lastly, Hidden Markov Model searches identified three protein family motifs, including cold shock domain proteins and fatty acid hydroxylases that were significantly associated with psychrotolerance in BHI broth. (
  • For example rescue of the cold-sensitive phenotype requires the 44-kDa ATPase domain name from Ssb. (
  • 3371). ProS2 is an approximately 23 kDa soluble tandem-dimer peptide tag derived from the N-terminal domain of Protein S, a soluble protein that originates from the myxobacterium species Myxococcus xanthus . (
  • ProS2 is approximately 23 kDa and is a tandem-dimer peptide derived from the N-terminal domain of the soluble myxobacterium Myxococcus xanthus Protein S. It is also expressed in the cold shock expression vector pCold ProS2 DNA (Cat. (
  • We show that in eukaryotes this domain is often combined in the same polypeptide with protein-protein- or lipid- interaction domains that might play a role in anchoring these proteins to specific cytoskeletal structures. (
  • Thus, proteins with this domain might have a key role in the recognition and localization of dsRNA, including miRNAs, rasiRNAs and piRNAs hybridized to their targets. (
  • In the second part (Chapter 4), the structural plasticity of the cold shock domain architecture is evaluated, by comparing the structure of a CSP domain- swapped dimer to closed-monomeric structures of CSP. (
  • The first step is the characterization of proteins from each functional domain. (
  • Inhibitor binding induces active site stabilization of the HCV NS3 protein serine protease domain. (
  • A multidomain protein, AHM1 has the special combination of a J domain-homologous region and a Zn finger-like motif (a J-Z array) and an AT hook. (
  • Under optimized conditions, a 34-kDa javanicin-intein fusion protein was expressed and approximately 2.5-3.5 mg/L of soluble recombinant javanicin was successfully extracted with over 90% purity. (