The FHA domain is a modular phosphopeptide recognition motif
The FHA domain is a modular phosphopeptide recognition motif
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DOI：
10.1016/s1097-2765(00)80340-8
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发表时间：
1999-09-01
期刊：
影响因子：
16
通讯作者：
Jackson, SP
中科院分区：
文献类型：
--
作者：
Durocher, D;Henckel, J;Jackson, SP
FHA 结构域是 65-100 个氨基酸残基的保守序列，主要存在于真核细胞核蛋白中，但也存在于某些原核生物中。 FHA 结构域被认为介导蛋白质-蛋白质相互作用，但其作用模式尚未阐明。在这里，我们发现酿酒酵母 Rad53p（一种参与细胞周期检查点控制的蛋白激酶）的两个高度不同的 FHA 结构域具有磷酸肽结合特异性。我们还证明其他 FHA 结构域以磷酸依赖性方式结合肽。这些发现表明，FHA 结构域是一种磷酸化特异性蛋白质-蛋白质相互作用基序，对真核生物和原核生物的细胞内信号传导机制具有重要意义。
FHA domains are conserved sequences of 65-100 amino acid residues found principally within eukaryotic nuclear proteins, but which also exist in certain prokaryotes. The FHA domain is thought to mediate protein-protein interactions, but its mode of action has yet to be elucidated. Here, we show that the two highly divergent FHA domains of Saccharomyces cerevisiae Rad53p, a protein kinase involved in cell cycle checkpoint control, possess phosphopeptide-binding specificity. We also demonstrate that other FHA domains bind peptides in a phospho-dependent manner. These findings indicate that the FHA domain is a phospho-specific protein-protein interaction motif and have important implications for mechanisms of intracellular signaling in both eukaryotes and prokaryotes.