VILLIN SEQUENCE AND PEPTIDE MAP IDENTIFY 6 HOMOLOGOUS DOMAINS
VILLIN SEQUENCE AND PEPTIDE MAP IDENTIFY 6 HOMOLOGOUS DOMAINS
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DOI：
10.1073/pnas.85.14.4986
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发表时间：
1988-07-01
影响因子：
11.1
通讯作者：
AHMED, Y
中科院分区：
文献类型：
--
作者：
BAZARI, WL;MATSUDAIRA, P;AHMED, Y
位点特异性蛋白酶和绒毛蛋白氨基末端的抗血清已经被用来表明绒毛蛋白被组织成七个蛋白酶抗性结构域。其中6个包含在氨基末端Mr 87,000绒毛蛋白核心中，这是一个Ca2+调节的肌动蛋白切断片段，而羧基末端结构域包括绒毛蛋白“头饰”，这是一个参与肌动蛋白细丝捆绑的片段。Ca2+抑制绒毛蛋白氨基末端一半结构域之间的蛋白水解裂解。从单个cDNA克隆中推断出的绒毛蛋白蛋白序列包含一个重复6次的保守序列，该序列存在于绒毛蛋白核心的每个结构域。保守的重复序列存在于其他切断肌动蛋白的蛋白中，但不存在于绒毛蛋白的头部。我们的研究结果表明，肌动蛋白切断蛋白是围绕一个共同的Mr 14000 - 17000结构域组织的。
Site-specific proteases and antisera to the amino terminus of villin have been used to show that villin is organized into seven protease-reistant domains. Six are contained in the amino-terminal Mr 87,000 villin core, a Ca2+-regulated actin-severing fragment, whereas the carboxyl-terminal domain includes the villin "headpiece", a fragment involved in bundling of actin filaments. Ca2+ inhibits proteolytic cleavage between domains in the amino-terminal half of villin. The protein sequence of villin deduced from a single cDNA clone contains a conserved sequence that is repeated six times and is found in each domain of the villin core. The conserved repeats are found in other actin-severing proteins but not in the villin headpiece. Our results suggest that actin-severing proteins are organized around a common Mr 14,000-17,000 domain.