Domain mapping of the Rad51 paralog protein complexes
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Domain mapping of the Rad51 paralog protein complexes
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| Id. |
17940264 |
| Idioma |
inglés
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| Titulo |
Domain mapping of the Rad51 paralog protein complexes |
| Autor(es) |
Miller, Kristi A.
Sawicka, Dorota
Barsky, Daniel
Albala, Joanna S.
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| Localización |
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=373258
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| Versión |
1.0 |
| Estado |
Final
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| Descripción |
The five human Rad51 paralogs are suggested to play an important role in the maintenance of genome stability through their function in DNA double-strand break repair. These proteins have been found to form two distinct complexes in vivo, Rad51Bâ??Rad51Câ??Rad51Dâ??Xrcc2 (BCDX2) and Rad51Câ??Xrcc3 (CX3). Based on the recent Pyrococcus furiosus Rad51 structure, we have used homology modeling to design deletion mutants of the Rad51 paralogs. The models of the human Rad51B, Rad51C, Xrcc3 and murine Rad51D (mRad51D) proteins reveal distinct N-terminal and C-terminal domains connected by a linker region. Using yeast two-hybrid and co-immunoprecipitation techniques, we have demonstrated that a fragment of Rad51B containing amino acid residues 1â??75 interacts with the C-terminus and linker of Rad51C, residues 79â??376, and this region of Rad51C also interacts with mRad51D and Xrcc3. We have also determined that the N-terminal domain of mRad51D, residues 4â??77, binds to Xrcc2 while the C-terminal domain of mRad51D, residues 77â??328, binds Rad51C. By this, we have identified the binding domains of the BCDX2 and CX3 complexes to further characterize the interaction of these proteins and propose a scheme for the three-dimensional architecture of the BCDX2 and CX3 paralog complexes.
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| Palabras clave |
Articles
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| Tipo de recurso |
Text
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| Tipo de Interactividad |
Expositivo
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| Nivel de Interactividad |
muy bajo
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| Audiencia |
Estudiante
Profesor
Autor
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| Estructura |
Atomic |
| Coste |
no
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| Copyright |
sí
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Copyright © 2004 Oxford University Press |
| Requerimientos técnicos |
Browser: Any
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| Fecha de contribución |
11-feb-2008 |
| Contacto |
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