Functional specificity among Hsp70 molecular chaperones.
Molecular chaperones of the 70-kilodalton heat shock protein (Hsp70) class bind to partially unfolded polypeptide substrates and participate in a wide variety of cellular processes. Differences in peptide-binding specificity among Hsp70s have led to the hypothesis that peptide binding determines specific Hsp70 functions. Protein domains were identified that were required for two separate functions of a yeast Hsp70 family. The peptide-binding domain was not required for either of these specific Hsp70 functions, which suggests that peptide-binding specificity plays little or no role in determining Hsp70 functions in vivo.
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Department of Biomolecular Chemistry, University of Wisconsin, Madison, WI 53706, USA. ecraig@facstaff.wisc.edu
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D000251:Adenosine Triphosphatases / Q000378:metabolism; D003080:Cold Temperature; D005656:Fungal Proteins / Q000737:chemistry / Q000378:metabolism*; D018840:HSP70 Heat-Shock Proteins / Q000737:chemistry / Q000378:metabolism*; D006921:Hygromycin B / Q000494:pharmacology; D010455:Peptides / Q000378:metabolism*; D010641:Phenotype; D011132:Polyribosomes / Q000378:metabolism; D011485:Protein Binding; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000187:drug effects / Q000502:physiology; D029701:Saccharomyces cerevisiae Proteins
D005656:Fungal Proteins; D018840:HSP70 Heat-Shock Proteins; D010455:Peptides; D011993:Recombinant Fusion Proteins; C095192:SSB1 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D006921:Hygromycin B; D000251:Adenosine Triphosphatases; C095973:SSA1 protein, S cerevisiae