Pathway leading to correctly folded beta-tubulin
Pathway leading to correctly folded beta-tubulin
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DOI：
10.1016/s0092-8674(00)80100-2
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发表时间：
1996-07-26
期刊：
影响因子：
64.5
通讯作者：
Cowan, NJ
中科院分区：
文献类型：
--
作者：
Tian, GL;Huang, Y;Cowan, NJ
我们描述了完整的β-微管蛋白折叠途径。通过ATP依赖性与胞质伴侣蛋白相互作用产生的折叠中间体经历与四种蛋白质（辅因子A、D、E和C）的一系列相互作用。在级联反应中的postchaperonin步骤不依赖于ATP或GTP水解，虽然GTP在微管蛋白折叠中起着结构性作用。辅因子A和D通过捕获和稳定准天然构象的β-微管蛋白发挥作用。辅因子E与辅因子D-β-微管蛋白复合物结合;然后与辅因子C相互作用导致β-微管蛋白多肽释放，其被定型为天然状态。序列分析鉴定了辅因子D（cin 1）和E（pac 2）的酵母同源物，其特征在于影响微管功能的突变。
We describe the complete beta-tubulin folding pathway. Folding intermediates produced via ATP-dependent interaction with cytosolic chaperonin undergo a sequence of interactions with four proteins (cofactors A, D, E, and C). The postchaperonin steps in the reaction cascade do not depend on ATP or GTP hydrolysis, although GTP plays a structural role in tubulin folding. Cofactors A and D function by capturing and stabilizing beta-tubulin in a quasi-native conformation. Cofactor E binds to the cofactor D-beta-tubulin complex; interaction with cofactor C then causes the release of beta-tubulin polypeptides that are committed to the native state. Sequence analysis identifies yeast homologs of cofactors D (cin1) and E (pac2), characterized by mutations that affect microtubule function.