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Nucleic Acids Research Advance Access originally published online on November 14, 2008
Nucleic Acids Research 2009 37(1):38-46; doi:10.1093/nar/gkn895
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Nucleic Acids Research, 2009, Vol. 37, No. 1 38-46
© 2008 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

Evidence for direct contact between the RPA3 subunit of the human replication protein A and single-stranded DNA

Tonatiuh Romero Salas1, Irina Petruseva2, Olga Lavrik2 and Carole Saintomé1,*

1Laboratoire de Biophysique Moléculaire, Cellulaire et Tissulaire, CNRS-ParisVI-Paris XIII-UMR 7033, 2 place Jussieu, 75251 Paris cedex 05, France and 2Institute of Chemical Biology and Fundamental Medicine, Prospekt Lavrentiev 8, 630090 Novosibirsk, Russia

*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 August 7, 2008. Revised October 20, 2008. Accepted October 26, 2008.

Replication Protein A is a single-stranded (ss) DNA-binding protein that is highly conserved in eukaryotes and plays essential roles in many aspects of nucleic acid metabolism, including replication, recombination, DNA repair and telomere maintenance. It is a heterotrimeric complex consisting of three subunits: RPA1, RPA2 and RPA3. It possesses four DNA-binding domains (DBD), DBD-A, DBD-B and DBD-C in RPA1 and DBD-D in RPA2, and it binds ssDNA via a multistep pathway. Unlike the RPA1 and RPA2 subunits, no ssDNA-RPA3 interaction has as yet been observed although RPA3 contains a structural motif found in the other DBDs. We show here using 4-thiothymine residues as photoaffinity probe that RPA3 interacts directly with ssDNA on the 3'-side on a 31 nt ssDNA.


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