DEFINING PROTEIN INTERACTIONS WITH YEAST ACTIN IN-VIVO
DEFINING PROTEIN INTERACTIONS WITH YEAST ACTIN IN-VIVO
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DOI：
10.1038/nsb0195-28
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发表时间：
1995-01-01
期刊：
影响因子：
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通讯作者：
BOTSTEIN, D
中科院分区：
文献类型：
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作者：
AMBERG, DC;BASART, E;BOTSTEIN, D
利用双杂交蛋白质相互作用报告系统，发现肌动蛋白、前纤维蛋白、Srv2p以及两种含SH3结构域的蛋白质在体内与酵母肌动蛋白结合。当检测其与分布在单体表面的35种肌动蛋白突变体相互作用的能力时，发现每种假定配体所特有的不同突变子集会破坏结合。特别是，肌动蛋白 - 肌动蛋白相互作用的差异相互作用模式与已发表的肌动蛋白丝结构一致。尽管功能相似，但Srv2p和前纤维蛋白的差异相互作用模式不同。相比之下，前纤维蛋白和SH3结构域蛋白质的模式表明存在一个共享的结合位点以及机制上的共性。
Using the two-hybrid protein interaction reporter system, actin, profilin, Srv2p and two SH3-containing proteins are found to bind yeast actin in vivo. When tested for ability to interact with 35 actin mutations distributed over the monomer surface, distinct subsets of mutations characteristic for each putative ligand are found to disrupt binding. In particular, the pattern of differential interactions for the actin-actin interaction is consistent with published structures for the actin filament. Despite functional similarities, the patterns of differential interaction for Srv2p and profilin are different. in contrast, the patterns for profilin and the SH3 domain proteins suggest a shared binding site and commonality in mechanism.