Key residues involved in Hsp70 regulatory activity and affect of co-chaperones on mechanism of action.
Hsp70 proteins assist refolding of polypeptides in an ATP dependent manner. Crystal structure of intact Hsp70 protein has not been determined yet however, structures of its two domains were solved separately. Allostery between ATPase domain and peptide-binding domain facilitates unfolded substrate processing. To elucidate function of key residues and affect of other factors involved in this allosteric mechanism, a biochemical study was undertaken.
Tutar
Yusuf
Y
Chemistry Department, Faculty of Science, Cumhuriyet University, Sivas 58140, Turkey. ytutar@cumhuriyet.edu.tr
D000596:Amino Acids / Q000235:genetics* / Q000378:metabolism*; D050956:HSP40 Heat-Shock Proteins / Q000378:metabolism; D018840:HSP70 Heat-Shock Proteins / Q000235:genetics* / Q000378:metabolism*; D009154:Mutation; D010843:Pichia; D017510:Protein Folding; D020673:Protein Renaturation; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism
D000596:Amino Acids; D050956:HSP40 Heat-Shock Proteins; D018840:HSP70 Heat-Shock Proteins; D029701:Saccharomyces cerevisiae Proteins; C070319:YDJ1 protein, S cerevisiae