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MBC in Press, published online ahead of print October 31, 2007
Mol. Biol. Cell 10.1091/mbc.E07-09-0961

A more recent version of this article appeared on January 1, 2008
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Submitted on September 24, 2007
Accepted on October 19, 2007

Regulation of Rtt107 Recruitment to Stalled DNA Replication Forks by the Cullin Rtt101 and the Rtt109 Acetyltransferase

Tania M. Roberts,* Iram Waris Zaidi,{dagger} Jessica A. Vaisica,* Matthias Peter,{dagger} and Grant W. Brown*

*Department of Biochemistry and Terrence Donnelly Centre for Cellular and Biomolecular Research, University of Toronto, Toronto, Ontario M5S 3E1, Canada; {dagger}Institute of Biochemistry, Eidgenössiche Technische Hochschule Zurich, 8093 Zurich, Switzerland

Monitoring Editor: Wendy Bickmore

RTT107 (ESC4, YHR154W) encodes a BRCA1 C-terminal-domain protein that is important for recovery from DNA damage during S phase. Rtt107 is a substrate of the checkpoint kinase Mec1 and forms complexes with DNA repair enzymes including the nuclease subunit Slx4, but the role of Rtt107 in the DNA damage response remains unclear. We find that Rtt107 interacts with chromatin when cells are treated with compounds that cause replication forks to arrest. This damage-dependent chromatin binding requires the acetyltransferase Rtt109, but does not require acetylation of the known Rtt109 target, histone H3-K56. Chromatin binding of Rtt107 also requires the cullin Rtt101, which appears to play a direct role in Rtt107 recruitment as the two proteins are found in complex with each other. Finally, we provide evidence that Rtt107 is bound at or near stalled replication forks in vivo. Together these results indicate that Rtt109, Rtt101, and Rtt107, which genetic evidence suggests are functionally related, form a DNA damage response pathway that recruits Rtt107 complexes to damaged or stalled replication forks.

Address correspondence to: Grant W. Brown (grant.brown{at}utoronto.ca)




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J. Fillingham, J. Recht, A. C. Silva, B. Suter, A. Emili, I. Stagljar, N. J. Krogan, C. D. Allis, M.-C. Keogh, and J. F. Greenblatt
Chaperone Control of the Activity and Specificity of the Histone H3 Acetyltransferase Rtt109
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