IDENTIFICATION OF A HUMAN CDNA-ENCODING A PROTEIN THAT IS STRUCTURALLY AND FUNCTIONALLY RELATED TO THE YEAST ADENYLYL CYCLASE-ASSOCIATED CAP PROTEINS
IDENTIFICATION OF A HUMAN CDNA-ENCODING A PROTEIN THAT IS STRUCTURALLY AND FUNCTIONALLY RELATED TO THE YEAST ADENYLYL CYCLASE-ASSOCIATED CAP PROTEINS
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DOI：
10.1128/mcb.12.11.5033
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发表时间：
1992-11-01
影响因子：
5.3
通讯作者：
YOUNG, D
中科院分区：
文献类型：
--
作者：
MATVIW, H;YU, G;YOUNG, D
酿酒酵母和粟酒裂殖酵母的腺苷酸环化酶都与名为CAP的相关蛋白质相关。In S.在酿酒酵母中，CAP是由RAS/环AMP途径介导的细胞应答所必需的。这两种酵母CAP似乎是双功能蛋白质：N-末端结构域是腺苷酸环化酶的正常功能所需的，而C-末端结构域的丢失导致似乎与cAMP途径无关的形态和营养缺陷。任一酵母CAP在异源酵母中的表达抑制与内源CAP的C-末端结构域的损失相关的表型，但不抑制N-末端结构域的损失。两个酵母CAP蛋白之间的同源性的基础上，我们设计了简并寡核苷酸，我们用来检测，通过聚合酶链反应方法，编码CAP相关肽的人cDNA片段。使用聚合酶链反应片段作为探针，我们分离出一个人的cDNA克隆编码一个475个氨基酸的蛋白质，是同源的酵母CAP蛋白。人CAP蛋白在S.酿酒酵母抑制与CAP的C-末端结构域的丢失相关的表型，但不抑制与N-末端结构域的丢失相关的表型。因此，CAP蛋白在酵母和哺乳动物之间的进化中在结构上和在一定程度上在功能上是保守的。
The adenylyl cyclases of both Saccharomyces cerevisiae and Schizosaccharomyces pombe are associated with related proteins named CAP. In S. cerevisiae, CAP is required for cellular responses mediated by the RAS/cyclic AMP pathway. Both yeast CAPs appear to be bifunctional proteins: the N-terminal domains are required for the proper function of adenylyl cyclase, while loss of the C-terminal domains results in morphological and nutritional defects that appear to be unrelated to the cAMP pathways. Expression of either yeast CAP in the heterologous yeast suppresses phenotypes associated with loss of the C-terminal domain of the endogenous CAP but does not suppress loss of the N-terminal domain. On the basis of the homology between the two yeast CAP proteins, we have designed degenerate oligonucleotides that we used to detect, by the polymerase chain reaction method, a human cDNA fragment encoding a CAP-related peptide. Using the polymerase chain reaction fragment as a probe, we isolated a human cDNA clone encoding a 475-amino-acid protein that is homologous to the yeast CAP proteins. Expression of the human CAP protein in S. cerevisiae suppresses the phenotypes associated with loss of the C-terminal domain of CAP but does not suppress phenotypes associated with loss of the N-terminal domain. Thus, CAP proteins have been structurally and, to some extent, functionally conserved in evolution between yeasts and mammals.