The FHA domain is a modular phosphopeptide recognition motif. |
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Authors: | D Durocher J Henckel A R Fersht S P Jackson |
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Institution: | Wellcome Trust and Cancer Research Campaign, Institute of Cancer and Developmental Biology, Cambridge, United Kingdom. |
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Abstract: | 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. |
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