Tuning of chaperone activity of Hsp70 proteins by modulation of nucleotide exchange

被引：176

作者：

Brehmer, D

Rüdiger, S

Gässler, CS

Klostermeier, D

Packschies, L

Reinstein, J

Mayer, MP

Bukau, B

机构：

[1] Univ Freiburg, Inst Biochem & Mol Biol, D-79104 Freiburg, Germany

[2] MRC Ctr, Cambridge Ctr Prot Engn, Cambridge CB2 2QH, England

[3] Scripps Res Inst, Dept Mol Biol, La Jolla, CA 92037 USA

[4] Max Planck Inst Mol Physiol, Phys Biochem Abt, D-44227 Dortmund, Germany

来源：

NATURE STRUCTURAL BIOLOGY | 2001年 / 8卷 / 05期

关键词：

D O I：

10.1038/87588

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

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 in these cycles by triggering substrate release. Structural searches of Hsp70 homologs revealed three structural elements within the ATPase domain: two salt bridges and an exposed loop. Mutational analysis showed that these elements control the dissociation of nucleotides, the interaction with exchange factors and chaperone activity Sequence variations in the three elements classify the Hsp70 family members into three subfamilies, DnaK proteins, HscA proteins and Hsc70 proteins. These subfamilies show strong differences in nucleotide dissociation and interaction with the exchange factors GrpE and Bag-1.

引用

收藏

页码：427 / 432

页数：6

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