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    Trends Biochem Sci. 2003 Feb;28(2):66-9.

    The THAP domain: a novel protein motif with similarity to the DNA-binding domain of P element transposase.

    Roussigne M, Kossida S, Lavigne AC, Clouaire T, Ecochard V, Glories A, Amalric F, Girard JP.

    Source

    Laboratoire de Biologie Vasculaire, Institut de Pharmacologie et de Biologie Structurale, CNRS UMR 5089, 205 route de Narbonne, 31077 Toulouse, France.

    Abstract

    We have identified a novel evolutionarily conserved protein motif - designated the THAP domain - that defines a new family of cellular factors. We have found that the THAP domain presents striking similarities with the site-specific DNA-binding domain (DBD) of Drosophila P element transposase, including a similar size, N-terminal location, and conservation of the residues that define the THAP motif, such as the C2CH signature (Cys-Xaa(2-4)-Cys-Xaa(35-50)-Cys-Xaa(2)-His). Our results suggest that the THAP domain is a novel example of a DBD that is shared between cellular proteins and transposases from mobile genomic parasites.

    PMID:
    12575992
    [PubMed - indexed for MEDLINE]

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