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DnaJ
In molecular biology, chaperone DnaJ, also known as Hsp40 (heat shock protein 40 kDa), is a molecular chaperone protein. It is expressed in a wide variety of organisms from bacteria to humans. Function Molecular chaperones are a diverse family of proteins that function to protect proteins from irreversible Protein aggregation, aggregation during synthesis and in times of cellular stress. The bacterial molecular chaperone Hsp70, DnaK is an enzyme that couples cycles of Adenosine triphosphate, ATP binding, hydrolysis, and Adenosine diphosphate, ADP release by an N-terminal ATP-hydrolyzing domain to cycles of sequestration and release of unfolded proteins by a C-terminal substrate binding domain. Dimeric GrpE is the co-chaperone for DnaK, and acts as a nucleotide exchange factor, stimulating the rate of ADP release 5000-fold. DnaK is itself a weak ATPase; ATP hydrolysis by DnaK is stimulated by its interaction with another co-chaperone, DnaJ. Thus the co-chaperones DnaJ and GrpE ar ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
DNAJA3
DnaJ homolog subfamily A member 3, mitochondrial, also known as Tumorous imaginal disc 1 (TID1), is a protein that in humans is encoded by the ''DNAJA3'' gene on chromosome 16. This protein belongs to the DNAJ/Hsp40 protein family, which is known for binding and activating Hsp70 chaperone (protein), chaperone proteins to perform protein folding, degradation, and complex assembly. As a mitochondrial protein, it is involved in maintaining membrane potential and mitochondrial DNA (mtDNA) integrity, as well as cellular processes such as cell movement, growth, and apoptosis, death. Furthermore, it is associated with a broad range of diseases, including neurodegenerative diseases, inflammatory diseases, and cancers. Structure As a member of the DNAJ/Hsp40 protein family, DNAJA3 contains a conserved DnaJ domain, which includes an HPD motif that interacts with Hsp70 to perform its cochaperone function. The DnaJ domain is composed of tetrahelical regions containing a tripeptide of histi ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
DNAJA1
DnaJ homolog subfamily A member 1 is a protein that in humans is encoded by the ''DNAJA1'' gene In biology, the word gene has two meanings. The Mendelian gene is a basic unit of heredity. The molecular gene is a sequence of nucleotides in DNA that is transcribed to produce a functional RNA. There are two types of molecular genes: protei .... Interactions DNAJA1 has been shown to interact with PTTG1. References Further reading * * * * * * * * * * * * * * * * * * Heat shock proteins {{gene-9-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
GrpE
GrpE (''Gro-P'' like protein E) is a bacterial nucleotide exchange factor that is important for regulation of protein folding machinery, as well as the heat shock response. It is a heat-inducible protein and during stress it prevents unfolded proteins from accumulating in the cytoplasm. Accumulation of unfolded proteins in the cytoplasm can lead to cell death. Discovery GrpE is a nucleotide exchange factor that was first discovered by researchers in 1977 as a protein necessary to propagate bacteriophage λ, a virus that infects bacteria by hijacking the bacteria's replication machinery, in ''Escherichia coli''. By using a genetic screen, researchers knocked out certain genes in E''. coli'' and then tested whether the bacteria was able to replicate, GrpE was found to be crucial to propagation. Since that time, GrpE has been identified in all bacteria and in Archaea where DnaK and DnaJ are present. The crystal structure of GrpE was determined in 1997 at 2.8 Angstrom and ide ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
DNAJB1
DnaJ homolog subfamily B member 1 is a protein that in humans is encoded by the ''DNAJB1'' gene. A fusion protein of DNAJB1 and PRKACA drives fibrolamellar hepatocellular carcinoma, a type of rare liver cancer. Interactions DNAJB1 has been shown to interact with: * HSPA4 Heat shock 70 kDa protein 4 is a protein that in humans is encoded by the ''HSPA4'' gene. The protein Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residue (biochemistry), residues. ..., and * STUB1 References Further reading * * * * * * * * * * * * * * * * * * Heat shock proteins {{gene-19-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
DNAJA2
DnaJ homolog subfamily A member 2 is a protein that in humans is encoded by the ''DNAJA2'' gene. The protein encoded by this gene shares sequence similarity with Hir1p and Hir2p, the two corepressors of histone gene transcription characterized in the yeast, Saccharomyces cerevisiae ''Saccharomyces cerevisiae'' () (brewer's yeast or baker's yeast) is a species of yeast (single-celled fungal microorganisms). The species has been instrumental in winemaking, baking, and brewing since ancient times. It is believed to have be .... The structural features of this protein suggest that it may function as part of a multiprotein complex. Several cDNAs encoding interacting proteins, HIRIPs, have been identified. HIRIP4 was isolated by virtue of its interaction with this protein; however, its exact function is not known. The sequence of HIRIP4 protein is highly homologous to the human DNJ3/ CPR3, mouse Dj3 and rat Dj2 gene products. References Further reading * * * * * * * * * * * ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Co-chaperone
Co-chaperones are proteins that assist chaperones in protein folding and other functions. Co-chaperones are the non-client binding molecules that assist in protein folding mediated by Hsp70 and Hsp90. They are particularly essential in stimulation of the ATPase activity of these chaperone proteins. There are a great number of different co-chaperones however based on their domain structure most of them fall into two groups: J-domain proteins and tetratricopeptide repeats (TPR). Co-chaperones assist heat shock proteins in the protein folding process. These co-chaperones can function in a number of ways. Primarily co-chaperones are involved in the ATPase functionality of their associated heat shock proteins. Co-chaperones catalyze the hydrolysis ATP to ADP on their respective chaperones which then allows them undergo a large conformational change that allows them to either bind to their substrates with higher affinity or aid in the release of the substrate following protein folding, ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Chaperone Protein
In molecular biology, molecular chaperones are proteins that assist the conformational folding or unfolding of large proteins or macromolecular protein complexes. There are a number of classes of molecular chaperones, all of which function to assist large proteins in proper protein folding during or after synthesis, and after partial denaturation. Chaperones are also involved in the translocation of proteins for proteolysis. The first molecular chaperones discovered were a type of assembly chaperones which assist in the assembly of nucleosomes from folded histones and DNA. One major function of molecular chaperones is to prevent the aggregation of misfolded proteins, thus many chaperone proteins are classified as heat shock proteins, as the tendency for protein aggregation is increased by heat stress. The majority of molecular chaperones do not convey any steric information for protein folding, and instead assist in protein folding by binding to and stabilizing folding intermedia ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
DNAJA4
DnaJ heat shock protein family (Hsp40) member A4 is a protein that in humans is encoded by the DNAJA4 gene In biology, the word gene has two meanings. The Mendelian gene is a basic unit of heredity. The molecular gene is a sequence of nucleotides in DNA that is transcribed to produce a functional RNA. There are two types of molecular genes: protei .... References Further reading {{gene-15-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Hsp70
The 70 kilodalton heat shock proteins (Hsp70s or DnaK) are a family of conserved ubiquitously expressed heat shock proteins. Proteins with similar structure exist in virtually all living organisms and play crucial roles in the development of cancer, neurodegeneration, apoptosis, regulating sleep, and much more. Intracellularly localized Hsp70s are an important part of the cell's machinery for protein folding, performing chaperoning functions, and helping to protect cells from the adverse effects of physiological stresses. Additionally, membrane-bound Hsp70s have been identified as a potential target for cancer therapies and their extracellularly localized counterparts have been identified as having both membrane-bound and membrane-free structures. There is lot of potential in the Hsp70 protein as a key therapeutic target for developing new drugs for the treatment of sleep disorders, cancer, neurodegeneration, and other related pathological conditions. Discovery Members of the ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein Aggregation
In molecular biology, protein aggregation is a phenomenon in which intrinsically disordered proteins, intrinsically-disordered or mis-folded proteins aggregate (i.e., accumulate and clump together) either intra- or extracellularly. Protein aggregates have been implicated in a wide variety of diseases known as amyloidoses, including Amyotrophic lateral sclerosis, ALS, Alzheimer's, Parkinson's and prion disease. After synthesis, proteins typically Protein folding, fold into a particular Protein tertiary structure, three-dimensional conformation that is the most Thermodynamic equilibrium, thermodynamically favorable: their native state. This folding process is driven by the hydrophobic effect: a tendency for hydrophobic (water-fearing) portions of the protein to shield themselves from the hydrophilic (water-loving) environment of the cell by burying into the interior of the protein. Thus, the exterior of a protein is typically hydrophilic, whereas the interior is typically hydrophob ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Heat Shock Protein
Heat shock proteins (HSPs) are a family of proteins produced by cells in response to exposure to stressful conditions. They were first described in relation to heat shock, but are now known to also be expressed during other stresses including exposure to cold, UV light and during wound healing or tissue remodeling. Many members of this group perform chaperone functions by stabilizing new proteins to ensure correct folding or by helping to refold proteins that were damaged by the cell stress. This increase in expression is transcriptionally regulated. The dramatic upregulation of the heat shock proteins is a key part of the heat shock response and is induced primarily by heat shock factor (HSF). HSPs are found in virtually all living organisms, from bacteria to humans. Heat shock proteins are named according to their molecular weight. For example, Hsp60, Hsp70 and Hsp90 (the most widely studied HSPs) refer to families of heat shock proteins on the order of 60, 70 and 90 kilo ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cysteine
Cysteine (; symbol Cys or C) is a semiessential proteinogenic amino acid with the chemical formula, formula . The thiol side chain in cysteine enables the formation of Disulfide, disulfide bonds, and often participates in enzymatic reactions as a nucleophile. Cysteine is chiral, but both D and L-cysteine are found in nature. LCysteine is a protein monomer in all biota, and D-cysteine acts as a signaling molecule in mammalian nervous systems. Cysteine is named after its discovery in urine, which comes from the urinary bladder or cyst, from Ancient Greek, Greek κύστις ''kýstis'', "bladder". The thiol is susceptible to oxidation to give the disulfide bond, disulfide derivative cystine, which serves an important structural role in many proteins. In this case, the symbol Cyx is sometimes used. The deprotonated form can generally be described by the symbol Cym as well. When used as a food additive, cysteine has the E number E920. Cysteine is Genetic code, encoded by the codo ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
