Polypeptide transfer from Hsp40 to Hsp70 molecular chaperones.

Polypeptide transfer from Hsp40 to Hsp70 molecular chaperones.
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DOI:
10.1016/j.tibs.2008.12.009
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发表时间:
2009-05
影响因子:
13.8
通讯作者:
Cyr DM
Cyr DM
中科院分区:
生物学1区
文献类型:
--
作者:
Summers DW;Douglas PM;Ramos CH;Cyr DM

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热休克蛋白40(Hsp40)共分子伴侣通过将非天然蛋白质结合和递送至热休克蛋白70(Hsp70)来帮助细胞蛋白质折叠和降解。底物从Hsp40 s转移到Hsp70的机制尚不清楚。最近的两项研究提供了新的细节,阐明了新的机制,底物识别热休克蛋白40和一个共同的机制,多肽转移到热休克蛋白70。
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.
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