70-kD Heat Shock Protein
[Heat Shock Protein 70 is a class of conserved molecular chaperone proteins in both prokaryotes and eukaryotic cells that may interact with polypeptides during the assembly processes to prevent the formation of nonfunctional structures. There are at least three HSP70 loci in the human genome, which map to chromosomes 6, 14, 21, and at least one other chromosome. Heat-shock proteins are expressed in response to a variety of stresses. The human HSP70 multi-gene family encodes highly conserved 70 kD proteins with structural and functional properties in common, but which vary in their response to metabolic stress. Some mRNAs are rapidly degraded through an AU-rich 3-prime untranslated region bound by AUF1, which complexes with HSC70, HSP70, EIF4G, and poly(A)-binding protein. The mRNA decay is associated with displacement of EIF4G from AUF1, ubiquitination of AUF1, and degradation. HSP70 blocks decay of AU-rich mRNAs and AUF1 protein. ( NCI )]
UMLS (NCI) C0243043- Amino Acid, Peptide, or Protein
- Biologically Active Substance
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