Hsp110 is a nucleotide-activated exchange factor for Hsp70

被引:119
作者
Andreasson, Claes [1 ]
Fiaux, Jocelyne [1 ]
Rampelt, Heike [1 ]
Mayer, Matthias P. [1 ]
Bukau, Bernd [1 ]
机构
[1] Univ Heidelberg, DKFZ ZBH Alliance, Zentrum Mol Biol, D-69120 Heidelberg, Germany
关键词
D O I
10.1074/jbc.M710063200
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Hsp110 proteins constitute a subfamily of the Hsp70 chaperones and are potent nucleotide exchange factors ( NEFs) for canonical Hsp70s of the eukaryotic cytosol. Here, we show that the NEF activity of the yeast Hsp110 homologue Sse1 itself is controlled by nucleotide. Nucleotide binding results in formation of a stabilized conformation of Sse1 that is required for association with the yeast Hsp70 Ssa1. The interaction triggers release of bound ADP from Ssa1, but nucleotide persists bound to Sse1 in the complex. Surprisingly, removal of this nucleotide does not affect the integrity of the complex. Instead, rebinding of ATP to the Hsp70 prompts the dissociation of the complex. Our data demonstrate that in contrast to previously characterized NEFs for Hsp70 chaperones, the NEF activity of Sse1 requires nucleotide binding and let us propose a new model for Hsp110 function.
引用
收藏
页码:8877 / 8884
页数:8
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