The THAP domain: a novel protein motif with similarity to the DNA-binding domain of P element transposase |
| |
Authors: | Roussigne Myriam Kossida Sophia Lavigne Anne-Claire Clouaire Thomas Ecochard Vincent Glories Alexandra Amalric François Girard Jean-Philippe |
| |
Affiliation: | 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. |
| |
Keywords: | |
本文献已被 PubMed 等数据库收录! |
|