Tuning of chaperone activity of Hsp70 proteins by modulation of nucleotide exchange
作者： Dirk Brehmer , Stefan Rüdiger , Claudia S. Gässler , Dagmar Klostermeier , Lars Packschies
DOI: 10.1038/87588
关键词: Chaperone activity 、 Hsp70 、 Mutational analysis 、 Biology 、 Nucleotide 、 ATPase 、 Dissociation (chemistry) 、 Biochemistry 、 Protein folding
摘要: The Hsp70 chaperone activity in protein folding is regulated by ATP-controlled cycles of substrate binding and release. Nucleotide exchange plays a key role these triggering Structural searches homologs revealed three structural elements within the ATPase domain: two salt bridges an exposed loop. Mutational analysis showed that control dissociation nucleotides, interaction with factors activity. Sequence variations classify family members into subfamilies, DnaK proteins, HscA proteins Hsc70 proteins. These subfamilies show strong differences nucleotide GrpE Bag-1.
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