Nucleic Acids Research Advance Access published online on July 25, 2008
Nucleic Acids Research, doi:10.1093/nar/gkn441
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Molecular Biology |
Srs2 removes deadly recombination intermediates independently of its interaction with SUMO-modified PCNA
1CEA–DSV-Institut de Radiobiologie Cellulaire et Moléculaire, UMR217 CNRS/CEA, F-92265 Fontenay aux Roses and 2Laboratoire de Microscopie Moléculaire et Cellulaire, UMR 8126, Interactions Moléculaires et Cancer CNRS-Université Paris Sud-Institut de Cancérologie Gustave Roussy, F-94805 Villejuif, France
*To whom correspondence should be addressed. Tel: +33 1 46 54 93 43; Fax: +33 1 46 54 88 59; Email: xavier.veaute{at}cea.fr
Received December 18, 2007. Revised June 3, 2008. Accepted June 26, 2008.
Saccharomyces cerevisiae Srs2 helicase plays at least two distinct functions. One is to prevent recombinational repair through its recruitment by sumoylated Proliferating Cell Nuclear Antigen (PCNA), evidenced in postreplication-repair deficient cells, and a second one is to eliminate potentially lethal intermediates formed by recombination proteins. Both actions are believed to involve the capacity of Srs2 to displace Rad51 upon translocation on single-stranded DNA (ssDNA), though a role of its helicase activity may be important to remove some toxic recombination structures. Here, we described two new mutants, srs2R1 and srs2R3, that have lost the ability to hinder recombinational repair in postreplication-repair mutants, but are still able to remove toxic recombination structures. Although the mutants present very similar phenotypes, the mutated proteins are differently affected in their biochemical activities. Srs2R1 has lost its capacity to interact with sumoylated PCNA while the biochemical activities of Srs2R3 are attenuated (ATPase, helicase, DNA binding and ability to displace Rad51 from ssDNA). In addition, crossover (CO) frequencies are increased in both mutants. The different roles of Srs2, in relation to its eventual recruitment by sumoylated PCNA, are discussed.
Present address: Thomas Robert, FIRC Institute of Molecular Oncology Foundation, Via Adamello 16, 20139 Milan, Italy
The author wish it to be known that, in their opinion, the first two authors should be regarded as joint First Authors.
CiteULike 
Connotea 
Del.icio.us What's this?
This article has been cited by other articles:
|
|
 |
|
  S. Colavito, M. Macris-Kiss, C. Seong, O. Gleeson, E. C. Greene, H. L. Klein, L. Krejci, and P. Sung Functional significance of the Rad51-Srs2 complex in Rad51 presynaptic filament disruption Nucleic Acids Res., November 1, 2009; 37(20): 6754 - 6764. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 R. C. Burgess, M. Lisby, V. Altmannova, L. Krejci, P. Sung, and R. Rothstein Localization of recombination proteins and Srs2 reveals anti-recombinase function in vivo J. Cell Biol., June 15, 2009; 185(6): 969 - 981. [Abstract] [Full Text] [PDF]
|
|