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Nucleic Acids Research 2005 33(18):5878-5886; doi:10.1093/nar/gki902
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Published online 13 October 2005

© The Author 2005. Published by Oxford University Press. All rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions{at}oxfordjournals.org

Article

The RING finger ATPase Rad5p of Saccharomyces cerevisiae contributes to DNA double-strand break repair in a ubiquitin-independent manner

Shuhua Chen1,2, Adelina A. Davies2, Daniel Sagan1 and Helle D. Ulrich1,2,*

1Max Planck Institute for Terrestrial Microbiology, Karl-von-Frisch-Strasse D-35043 Marburg, Germany 2Cancer Research UK, London Research Institute, Clare Hall Laboratories Blanche Lane, South Mimms, Herts EN6 3LD, UK

*To whom correspondence should be addressed. Tel: +44 1707 62 5821; Fax: +44 1707 62 5550; Email: helle.ulrich{at}cancer.org.uk

Received August 17, 2005. Revised September 28, 2005. Accepted September 28, 2005.

Tolerance to replication-blocking DNA lesions is achieved by means of ubiquitylation of PCNA, the processivity clamp for replicative DNA polymerases, by components of the RAD6 pathway. In the yeast Saccharomyces cerevisiae the ubiquitin ligase (E3) responsible for polyubiquitylation of the clamp is the RING finger protein Rad5p. Interestingly, the RING finger, responsible for the protein's E3 activity, is embedded in a conserved DNA-dependent ATPase domain common to helicases and chromatin remodeling factors of the SWI/SNF family. Here, we demonstrate that the Rad5p ATPase domain provides the basis for a function of the protein in DNA double-strand break repair via a RAD52- and Ku-independent pathway mediated by the Mre11/Rad50/Xrs2 protein complex. This activity is distinct and separable from the contribution of the RING domain to ubiquitin conjugation to PCNA. Moreover, we show that the Rad5 protein physically associates with the single-stranded DNA regions at a processed double-strand break in vivo. Our observations suggest that Rad5p is a multifunctional protein that—by means of independent enzymatic activities inherent in its RING and ATPase domains—plays a modulating role in the coordination of repair events and replication fork progression in response to various different types of DNA lesions.

Present address: Daniel Sagan, GSF National Research Center for Environment and Health, Neuherberg, Germany


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