CDC16P, CDC23P AND CDC27P FORM A COMPLEX ESSENTIAL FOR MITOSIS
CDC16P, CDC23P AND CDC27P FORM A COMPLEX ESSENTIAL FOR MITOSIS
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DOI：
10.1002/j.1460-2075.1994.tb06752.x
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发表时间：
1994-09-15
期刊：
影响因子：
11.4
通讯作者：
HIETER, PA
中科院分区：
文献类型：
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作者：
LAMB, JR;MICHAUD, WA;HIETER, PA
Cdc 16 p、Cdc 23 p和Cdc 27 p是酿酒酵母细胞有丝分裂所必需的蛋白质。所有这三种蛋白质都含有多个串联重复的34个氨基酸的三肽重复序列（TPR）。使用两个独立的测定，在体内和体外免疫共沉淀的双杂交分析，我们证明，Cdc 16 p，Cdc 23 p和Cdc 27 p自我关联和相互作用，形成一个大分子复合物。在Cdc 27 p的最高度保守的TPR结构域中的温度敏感性突变导致与Cdc 23 p相互作用的能力大大降低，但对与野生型Cdc 27 p或Cdc 16 p的相互作用没有影响。这种效应的特异性表明，TPRs可以介导蛋白质-蛋白质相互作用，并且这种突变可能定义了酵母细胞周期进程的基本相互作用。从酵母到人类，这三种蛋白质中至少有两种是保守的，这表明这种蛋白质复合物对广泛的真核生物中的有丝分裂是必不可少的。
Cdc16p, Cdc23p and Cdc27p are all essential proteins required for cell cycle progression through mitosis in Saccharomyces cerevisiae. All three proteins contain multiple tandemly repeated 34 amino acid tetratrico-peptide repeats (TPRs). Using two independent assays, two-hybrid analysis in vivo and co-immunoprecipitation in vitro, we demonstrate that Cdc16p, Cdc23p and Cdc27p self associate and interact with one another to form a macromolecular complex. A temperature sensitive mutation in the most highly conserved TPR domain of Cdc27p results in a greatly reduced ability to interact with Cdc23p, but has no effect on interactions with wild-type Cdc27p or Cdc16p. The specificity of this effect indicates that TPRs can mediate protein-protein interactions and that this mutation may define an essential interaction for cell cycle progression in yeast. The conservation of at least two of the three proteins from yeast to man suggests that this protein complex is essential for mitosis in a wide range of eukaryotes.