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Nucleic Acids Research Advance Access originally published online on September 14, 2006
Nucleic Acids Research 2006 34(17):4857-4865; doi:10.1093/nar/gkl564
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Nucleic Acids Research, 2006, Vol. 34, No. 17 4857-4865
© 2006 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Nucleic Acid Enzymes

Human replication protein A unfolds telomeric G-quadruplexes

Tonatiuh Romero Salas, Irina Petruseva1, Olga Lavrik1, Anne Bourdoncle2, Jean-Louis Mergny2, Alain Favre and Carole Saintomé*

Institut Jacques Monod, CNRS-ParisVI-ParisVII-UMR 7592 2 place Jussieu, 75251 Paris cedex 05, France 1 Novosibirsk Institute of Bioorganic Chemistry, Siberian Division of Russian Academy of Sciences 630090 Novosibirsk, Russia 2 Laboratoire de Biophysique, INSERM U565, CNRS UMR 5153, Muséum National d'Histoire Naturelle USM 503 43 rue Cuvier, 75005 Paris, France

*To whom correspondence should be addressed. Tel: +33 1 44 27 40 86; Fax: +33 1 44 27 57 16; Email: saintome{at}ijm.jussieu.fr

Received June 15, 2006. Revised July 17, 2006. Accepted July 19, 2006.

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 conditions, 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 formation 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.


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