A Conserved HPD Sequence of the J-domain Is Necessary for YDJ1 Stimulation of Hsp70 ATPase Activity at a Site Distinct from Substrate Binding
作者： Joyce Tsai , Michael G. Douglas
关键词: Biochemistry 、 Binding site 、 Protein folding 、 Conserved sequence 、 A-site 、 Peptide sequence 、 Biology 、 DNAJ Protein 、 DNAJB1 、 Chaperone (protein)
摘要: The 46-kDa protein YDJ1 is one of several known yeast homologues the Escherichia coli DnaJ protein. Like all J homologues, it shares homology with highly conserved NH2-terminal "J-domain" DnaJ. A component DnaK (Hsp70) chaperone machinery that mediates folding, necessary for survival at elevated temperatures. It stimulates ATP hydrolysis by and effects release DnaK-bound polypeptides. Previous genetic biochemical studies indicate J-domain these functions. Using peptides corresponding to sequence, we show a peptide containing His-Pro-Asp sequence positions 34-36 in competes off stimulation Hsp70 ATPase activity. Inhibitory concentrations do not prevent binding folding substrates, therefore must interact site distinct from substrate binding. This interaction critical activity, since mutant harboring H34Q change (ydj1Q34) neither nor release. importance proper function this region supported poor growth temperature-sensitive phenotype expressing ydj1Q34.
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