編者按：今天出版的Science發(fā)表有關(guān)HSP70一篇文章,，為人類認(rèn)識(shí)這個(gè)老蛋白HSP70更進(jìn)一步。
Coordinated Activation of Hsp70 Chaperones
Gregor J. Steel, Donna M. Fullerton, John R. Tyson, Colin J. Stirling*
Hsp70s are a ubiquitous family of molecular chaperones involved in many cellular processes. Two Hsp70s, Lhs1p and Kar2p, are required for protein biogenesis in the yeast endoplasmic reticulum. Here, we found that Lhs1p and Kar2p specifically interacted to couple, and coordinately regulate, their respective activities. Lhs1p stimulated Kar2p by providinga specific nucleotide exchange activity, whereas Kar2p reciprocally activated the Lhs1p adenosine triphosphatase (ATPase). The two ATPase activities are coupled, and their coordinated regulation is essential for normal function in vivo.
School of Biological Sciences, University of Manchester, Manchester M13 9PT, UK.
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