伴侣蛋白决定热休克蛋白70的多种功能。

Partner proteins determine multiple functions of Hsp70.

作者信息

Rassow J, Voos W, Pfanner N

机构信息

Biochemisches Institut, Universität Freiburg, Hermann-HerderStrasse 7, D-79104 Freiburg, Germany.

出版信息

Trends Cell Biol. 1995 May;5(5):207-12. doi: 10.1016/s0962-8924(00)89001-7.

DOI:10.1016/s0962-8924(00)89001-7

PMID:14731451

Abstract

The 70 kDa heat shock proteins (Hsp70s) are ubiquitous molecular chaperones that are best known for their participation in protein folding. However, evidence is accumulating that Hsp70s perform several other cellular functions in cooperation with specific soluble or membrane-bound partner proteins. While the basic function of Hsp70s is explained by their ability to bind unfolded polypeptide segments, the partner proteins appear to customize them for specific roles such as involvement in protein traffic and folding, translocation of preproteins across membranes, and gene regulation.

摘要

70 kDa热休克蛋白（Hsp70s）是普遍存在的分子伴侣，因其参与蛋白质折叠而最为人所知。然而，越来越多的证据表明，Hsp70s与特定的可溶性或膜结合伴侣蛋白协同发挥其他几种细胞功能。虽然Hsp70s的基本功能可以通过其结合未折叠多肽片段的能力来解释，但伴侣蛋白似乎使其具备特定功能，如参与蛋白质运输和折叠、前体蛋白跨膜转运以及基因调控。