| Literature DB >> 12575992 |
Myriam Roussigne1, Sophia Kossida, Anne-Claire Lavigne, Thomas Clouaire, Vincent Ecochard, Alexandra Glories, François Amalric, Jean-Philippe Girard.
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.Entities:
Mesh:
Substances:
Year: 2003 PMID: 12575992 DOI: 10.1016/S0968-0004(02)00013-0
Source DB: PubMed Journal: Trends Biochem Sci ISSN: 0968-0004 Impact factor: 13.807