Mol Cell. 1999 Sep;4(3):387-94.

The FHA domain is a modular phosphopeptide recognition motif.

Durocher D, Henckel J, Fersht AR, Jackson SP.

Source

Wellcome Trust and Cancer Research Campaign, Institute of Cancer and Developmental Biology, Cambridge, United Kingdom.

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.

PMID:: 10518219; [PubMed - indexed for MEDLINE]

Publication Types, MeSH Terms, Substances, Grant Support

Publication Types

Research Support, Non-U.S. Gov't

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Wellcome Trust/United Kingdom

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Saccharomyces Genome Database

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