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Rtt109 acetylates histone H3 lysine 56 and functions in DNA replication
被引:345
作者:

Han, Junhong
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机构: Mayo Clin, Coll Med, Dept Biochem & Mol Biol, Rochester, MN 55905 USA

Zhou, Hui
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机构: Mayo Clin, Coll Med, Dept Biochem & Mol Biol, Rochester, MN 55905 USA

Horazdovsky, Bruce
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机构: Mayo Clin, Coll Med, Dept Biochem & Mol Biol, Rochester, MN 55905 USA

Zhang, Kangling
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机构: Mayo Clin, Coll Med, Dept Biochem & Mol Biol, Rochester, MN 55905 USA

Xu, Rui-Ming
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机构: Mayo Clin, Coll Med, Dept Biochem & Mol Biol, Rochester, MN 55905 USA

Zhang, Zhiguo
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机构: Mayo Clin, Coll Med, Dept Biochem & Mol Biol, Rochester, MN 55905 USA
机构:
[1] Mayo Clin, Coll Med, Dept Biochem & Mol Biol, Rochester, MN 55905 USA
[2] Univ Calif Riverside, Mass Spectrometry Facil, Riverside, CA 92521 USA
[3] NYU, Sch Med, Struct Biol Program,Skirball Inst Biomed, Helen L & Martin S Kimmel Ctr Biol & Med, New York, NY 10016 USA
[4] NYU, Sch Med, Dept Pharmacol, New York, NY 10016 USA
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D O I:
10.1126/science.1133234
中图分类号:
O [数理科学和化学];
P [天文学、地球科学];
Q [生物科学];
N [自然科学总论];
学科分类号:
07 ;
0710 ;
09 ;
摘要:
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.
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页码:653 / 655
页数:3
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