An atlas of chaperone-protein interactions in Saccharomyces cerevisiae: implications to protein folding pathways in the cell.

An atlas of chaperone-protein interactions in Saccharomyces cerevisiae: implications to protein folding pathways in the cell.
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DOI:
10.1038/msb.2009.26
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发表时间:
2009
影响因子:
9.9
通讯作者:
Houry, Walid A.
Houry, Walid A.
中科院分区:
生物学1区
文献类型:
--
作者:
Gong, Yunchen;Kakihara, Yoshito;Krogan, Nevan;Greenblatt, Jack;Emili, Andrew;Zhang, Zhaolei;Houry, Walid A.

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分子伴侣参与了许多细胞功能,然而,对分子伴侣及其辅因子和底物之间相互作用的详细和全面的概述仍然缺乏。系统分析了酿酒酵母中所有已知的63个伴侣分子基于物理TAP-Tag的蛋白质-蛋白质相互作用。这些分子伴侣包括7个小分子热休克蛋白、3个AAA+家族成员、8个CCT/TIC复合体成员、6个前折叠蛋白/GimC复合体成员、22个Hsp40蛋白、1个Hsp60蛋白、14个Hsp70蛋白和2个Hsp90蛋白。我们的分析提供了功能混杂的伴侣和功能特定的伴侣之间的明显区别。我们发现,一种给定的蛋白质在细胞内的生命周期中可以与多达25种不同的伴侣相互作用。相互作用的伴侣的数量被发现随着给定蛋白质中长度在1到5之间的疏水延伸的平均数量而增加。重要的是,阐明了分子伴侣相互作用的细胞热点。我们的数据表明细胞中存在内源性多组分伴侣模块。
Molecular chaperones are known to be involved in many cellular functions, however, a detailed and comprehensive overview of the interactions between chaperones and their cofactors and substrates is still absent. Systematic analysis of physical TAP-tag based protein–protein interactions of all known 63 chaperones in Saccharomyces cerevisiae has been carried out. These chaperones include seven small heat-shock proteins, three members of the AAA+ family, eight members of the CCT/TRiC complex, six members of the prefoldin/GimC complex, 22 Hsp40s, 1 Hsp60, 14 Hsp70s, and 2 Hsp90s. Our analysis provides a clear distinction between chaperones that are functionally promiscuous and chaperones that are functionally specific. We found that a given protein can interact with up to 25 different chaperones during its lifetime in the cell. The number of interacting chaperones was found to increase with the average number of hydrophobic stretches of length between one and five in a given protein. Importantly, cellular hot spots of chaperone interactions are elucidated. Our data suggest the presence of endogenous multicomponent chaperone modules in the cell.
Pfam:氏族、网络工具和服务。
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影响因子: 14.9
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