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Human replication protein A unfolds telomeric G-quadruplexes (2006)
| Content Provider | CiteSeerX |
|---|---|
| Author | Favre, Alain Mergny, Jean-Louis Lavrik, Olga Bourdoncle, Anne Petruseva, Irina Salas, Tonatiuh Romero |
| Abstract | G-quadruplex structures inhibit telomerase activity and must be disrupted for telomere elongation during S phase. It has been suggested that the replication protein A (RPA) could unwind and maintain single-stranded DNA in a state amenable to the binding of telomeric components. We show here that under near-physiological in vitro condi-tions, human RPA is able to bind and unfold G-quadruplex structures formed from a 21mer human telomeric sequence. Analyses by native gel electrophoresis, cross-linking and fluorescence resonance energy transfer indicate the forma-tion of both 1:1 and 2:1 complexes in which G-quadruplexes are unfolded. In addition, quadruplex opening by hRPA is much faster than observed with the complementary DNA, demonstrating that this protein efficiently unfolds G-quartets. A two-step mechanism accounting for the binding of hRPA to G-quadruplexes is proposed. These data point to the involvement of hRPA in regulation of telomere maintenance. |
| File Format | |
| Journal | Nucleic Acids Res |
| Publisher Date | 2006-01-01 |
| Access Restriction | Open |
| Subject Keyword | Vitro Condi-tions Human Rpa Telomere Maintenance Native Gel Electrophoresis Single-stranded Dna Telomere Elongation Unfolds G-quartets Quadruplex Opening Unfold G-quadruplex Structure Complementary Dna G-quadruplex Structure Inhibit Telomerase Activity Fluorescence Resonance Energy Transfer Human Telomeric Sequence Two-step Mechanism Accounting Telomeric Component |
| Content Type | Text |
