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

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, inclu...

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Bibliographic Details
Published in:Trends in biochemical sciences (Amsterdam. Regular ed.) 2003-02, Vol.28 (2), p.66-69
Main Authors: Roussigne, Myriam, Kossida, Sophia, Lavigne, Anne-Claire, Clouaire, Thomas, Ecochard, Vincent, Glories, Alexandra, Amalric, François, Girard, Jean-Philippe
Format: Article
Language:English
Subjects:
Amino Acid Motifs
Amino Acid Sequence
Animals
Binding Sites
DNA-Binding Proteins - genetics
DNA-Binding Proteins - metabolism
Drosophila melanogaster - enzymology
Drosophila melanogaster - genetics
Humans
Life Sciences
Molecular Sequence Data
Protein Binding
Protein Structure, Tertiary
Sequence Homology, Amino Acid
Transposases - genetics
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Summary: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.
ISSN:0968-0004
1362-4326
DOI:10.1016/S0968-0004(02)00013-0