Chaperonins--keeping a lid on folding proteins.
Chaperonins--keeping a lid on folding proteins.
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伴侣蛋白——抑制蛋白质折叠。
DOI：
10.1016/s0014-5793(01)02838-1
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发表时间：
2001
期刊：
影响因子：
3.5
通讯作者：
Martin,J
中科院分区：
文献类型：
--
作者：
Kusmierczyk,AR;Martin,J
已知在所有生物体中，有两类伴侣参与新合成蛋白质的折叠。尽管细菌I型伴侣蛋白使用可逆结合的辅因子来暂时将折叠底物蛋白隔离在圆柱形伴侣素腔内，但古生菌和真核细胞胞质中的II型伴侣蛋白似乎已经进化出一个内置的盖子来实现这一目的。这并不完全令人惊讶，这对这两种类型的伴侣蛋白的折叠模式有影响。
Two classes of chaperonins are known in all groups of organisms to participate in the folding of newly synthesized proteins. Whereas bacterial type I chaperonins use a reversibly binding cofactor to temporarily sequester folding substrate proteins within the cylindrical chaperonin cavity, type II chaperonins in archaea and the eukaryotic cytosol appear to have evolved a built-in lid for this purpose. Not entirely surprisingly, this has consequences for the folding modes of the two types of chaperonins.