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Science 2 February 2007:
Vol. 315. no. 5812, pp. 653 - 655
DOI: 10.1126/science.1133234
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Reports

Rtt109 Acetylates Histone H3 Lysine 56 and Functions in DNA Replication

Junhong Han,1 Hui Zhou,1 Bruce Horazdovsky,1 Kangling Zhang,2 Rui-Ming Xu,3 Zhiguo Zhang1*

Acetylation of histone H3 lysine 56 (H3-K56) occurs in S phase, and cells lacking H3-K56 acetylation are sensitive to DNA-damaging agents. However, the histone acetyltransferase (HAT) that catalyzes global H3-K56 acetylation has not been found. Here we show that regulation of Ty1 transposition gene product 109 (Rtt109) is an H3-K56 HAT. Cells lacking Rtt109 or expressing rtt109 mutants with alterations at a conserved aspartate residue lose H3-K56 acetylation and exhibit increased sensitivity toward genotoxic agents, as well as elevated levels of spontaneous chromosome breaks. Thus, Rtt109, which shares no sequence homology with any other known HATs, is a unique HAT that acetylates H3-K56.

1 Department of Biochemistry and Molecular Biology, Mayo Clinic College of Medicine, 200 First Street SW, Rochester, MN 55905, USA.
2 Mass Spectrometry Facility, University of California at Riverside, Riverside, CA 92521, USA.
3 Structural Biology Program, Helen L. and Martin S. Kimmel Center for Biology and Medicine, Skirball Institute of Biomedicine and Department of Pharmacology, New York University School of Medicine, 540 First Avenue, New York, NY 10016, USA.

* To whom correspondence should be addressed. E-mail: Zhang.Zhiguo{at}mayo.edu

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