多肽从热休克蛋白40（Hsp40）转移至热休克蛋白70（Hsp70）分子伴侣。
Polypeptide transfer from Hsp40 to Hsp70 molecular chaperones.
作者信息
Summers Daniel W, Douglas Peter M, Ramos Carlos H I, Cyr Douglas M
机构信息
Department of Cell and Developmental Biology, University of North Carolina at Chapel Hill, NC 27599-7090, USA.
出版信息
Trends Biochem Sci. 2009 May;34(5):230-3. doi: 10.1016/j.tibs.2008.12.009. Epub 2009 Apr 7.
Abstract
Heat shock protein 40 (Hsp40) co-chaperones assist in cellular protein folding and degradation through the binding and delivery of non-native proteins to heat shock protein 70 (Hsp70). The mechanism for substrate transfer from Hsp40s to Hsp70 is unknown. Two recent studies provide new details that shed light on novel mechanisms for substrate recognition by Hsp40s and a common mechanism for polypeptide transfer to Hsp70.
摘要
热休克蛋白40（Hsp40）共伴侣蛋白通过将非天然蛋白质结合并递送至热休克蛋白70（Hsp70）来协助细胞内蛋白质折叠和降解。底物从Hsp40转移至Hsp70的机制尚不清楚。最近的两项研究提供了新的细节，揭示了Hsp40识别底物的新机制以及多肽转移至Hsp70的共同机制。
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