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Molecular and Cellular Biology, November 2006, p. 8396-8409, Vol. 26, No. 22
0270-7306/06/$08.00+0     doi:10.1128/MCB.01317-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Phosphorylation of Rad55 on Serines 2, 8, and 14 Is Required for Efficient Homologous Recombination in the Recovery of Stalled Replication Forks^,

Kristina Herzberg,^1, Vladimir I. Bashkirov,^1,, Michael Rolfsmeier,^1,# Edwin Haghnazari,^1,¶ W. Hayes McDonald,^2,|| Scott Anderson,² Elena V. Bashkirova,^1, John R. Yates III,² and Wolf-Dietrich Heyer^1,3*

Sections of Microbiology,¹ Molecular and Cellular Biology, Center for Genetics and Development, University of California, Davis, California 95616-8665,³ Department of Cell Biology, SR-11, Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92307²

Received 18 July 2006/ Returned for modification 2 August 2006/ Accepted 28 August 2006

DNA damage checkpoints coordinate the cellular response to genotoxic stress and arrest the cell cycle in response to DNA damage and replication fork stalling. Homologous recombination is a ubiquitous pathway for the repair of DNA double-stranded breaks and other checkpoint-inducing lesions. Moreover, homologous recombination is involved in postreplicative tolerance of DNA damage and the recovery of DNA replication after replication fork stalling. Here, we show that the phosphorylation on serines 2, 8, and 14 (S2,8,14) of the Rad55 protein is specifically required for survival as well as for normal growth under genome-wide genotoxic stress. Rad55 is a Rad51 paralog in Saccharomyces cerevisiae and functions in the assembly of the Rad51 filament, a central intermediate in recombinational DNA repair. Phosphorylation-defective rad55-S2,8,14A mutants display a very slow traversal of S phase under DNA-damaging conditions, which is likely due to the slower recovery of stalled replication forks or the slower repair of replication-associated DNA damage. These results suggest that Rad55-S2,8,14 phosphorylation activates recombinational repair, allowing for faster recovery after genotoxic stress.

Published ahead of print on 11 September 2006.

Supplemental material for this article may be found at http://mcb.asm.org/.

These authors made equal contributions and share first authorship.

Present address: Applied Biosystems, Foster City, CA 94404.

^# Present address: School of Molecular Biosciences, Washington State University, Pullman, WA 99163.

^¶ Present address: Scios, Inc., Fremont, CA 94555.

^|| Present address: Oak Ridge National Laboratory, Oak Ridge, TN 37831.

Present address: Novozymes Biotech, Inc., Davis, CA 95616.

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