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翻译后蛋白质的导入与折叠。

Post-translational protein import and folding.

作者信息

Höhfeld J, Hartl F U

机构信息

Howard Hughes Medical Institute, New York.

出版信息

Curr Opin Cell Biol. 1994 Aug;6(4):499-509. doi: 10.1016/0955-0674(94)90068-x.

DOI:10.1016/0955-0674(94)90068-x
PMID:7986525
Abstract

Significant advances have been made over the past year in analyzing the membrane machineries for the post-translational export of proteins in bacteria and for the import of proteins into mitochondria. Another important development is the identification in mitochondria of homologs of the bacterial heat-shock proteins DnaJ and GrpE, which function together with Hsp70 in membrane translocation and folding of imported proteins. A number of gene products involved in peroxisomal protein uptake have been identified, which are now awaiting biochemical analysis.

摘要

在过去一年里,在分析细菌中蛋白质翻译后输出的膜机制以及蛋白质导入线粒体的机制方面取得了重大进展。另一个重要进展是在线粒体中鉴定出细菌热休克蛋白DnaJ和GrpE的同源物,它们与Hsp70一起在导入蛋白质的膜易位和折叠中发挥作用。已经鉴定出一些参与过氧化物酶体蛋白质摄取的基因产物,目前正等待进行生化分析。

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Post-translational protein import and folding.翻译后蛋白质的导入与折叠。
Curr Opin Cell Biol. 1994 Aug;6(4):499-509. doi: 10.1016/0955-0674(94)90068-x.
2
The effects of chaperones and the influence of protein assembly on peroxisomal protein import.伴侣蛋白的作用以及蛋白质组装对过氧化物酶体蛋白质输入的影响。
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Control of folding and membrane translocation by binding of the chaperone DnaJ to nascent polypeptides.伴侣蛋白DnaJ与新生多肽结合对折叠和膜易位的调控。
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Temperature-controlled activity of DnaK-DnaJ-GrpE chaperones: protein-folding arrest and recovery during and after heat shock depends on the substrate protein and the GrpE concentration.DnaK-DnaJ-GrpE伴侣蛋白的温度控制活性:热休克期间及之后的蛋白质折叠停滞与恢复取决于底物蛋白和GrpE浓度。
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ClpB and HtpG facilitate de novo protein folding in stressed Escherichia coli cells.ClpB和HtpG有助于应激条件下的大肠杆菌细胞中的新生蛋白质折叠。
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Molecular chaperones as essential mediators of mitochondrial biogenesis.分子伴侣作为线粒体生物发生的关键介质。
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Heat shock proteins hsp60 and hsp70: their roles in folding, assembly and membrane translocation of proteins.热休克蛋白hsp60和hsp70:它们在蛋白质折叠、组装及膜转运中的作用。
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