Inhibitory effects of HSP70 chaperones on nascent polypeptides.
Inhibitory effects of HSP70 chaperones on nascent polypeptides.
复制标题
HSP70 伴侣对新生多肽的抑制作用。
DOI：
10.1002/pro.5560010803
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发表时间：
1992
期刊：
影响因子：
--
通讯作者：
Schlesinger,MJ
中科院分区：
文献类型：
--
作者：
Ryan,C;Stevens,TH;Schlesinger,MJ
Several of the major heat shock proteins (HSPs) function normally as molecular chaperones to prevent aggregation of immature polypeptides and thereby facilitate folding and oligomerization. To determine their effect on nascent polypeptides, we added purified preparations of different isoforms of HSP70 to in vitro translation reactions primed by the 26S mRNA of Sindbis virus, which encodes an autoprotease that functions cotranslationally, or by the mRNA encoding the yeast vacuolar H+ATPase, which is formed by a novel transpeptidase activity that removes the central region of the initial polypeptide. In the presence of HSP70s both the autoprotease and transpeptidase activities were inhibited, indicating that these chaperones can interact with nascent polypeptides and, in the cases studied here, perturb their normal structures.
