SIRT6 Promotes DNA Repair Under Stress by Activating PARP1

被引：659

作者：

Mao, Zhiyong ^{[1
]}

Hine, Christopher ^{[1
]}

Tian, Xiao ^{[1
]}

Van Meter, Michael ^{[1
]}

Au, Matthew ^{[1
]}

Vaidya, Amita ^{[1
]}

Seluanov, Andrei ^{[1
]}

Gorbunova, Vera ^{[1
]}

机构：

[1] Univ Rochester, Dept Biol, Rochester, NY 14627 USA

来源：

SCIENCE | 2011年 / 332卷 / 6036期

关键词：

DOUBLE-STRAND BREAKS; HOMOLOGOUS RECOMBINATION; PROTEIN SIR2; DEACETYLASE; STABILITY; CHROMATIN; POLY(ADP-RIBOSYL)ATION; LONGEVITY; KINASE; SITES;

D O I：

10.1126/science.1202723

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：

Sirtuin 6 (SIRT6) is a mammalian homolog of the yeast Sir2 deacetylase. Mice deficient for SIRT6 exhibit genome instability. Here, we show that in mammalian cells subjected to oxidative stress SIRT6 is recruited to the sites of DNA double-strand breaks (DSBs) and stimulates DSB repair, through both nonhomologous end joining and homologous recombination. Our results indicate that SIRT6 physically associates with poly[adenosine diphosphate (ADP)-ribose] polymerase 1 (PARP1) and mono-ADP-ribosylates PARP1 on lysine residue 521, thereby stimulating PARP1 poly-ADP-ribosylase activity and enhancing DSB repair under oxidative stress.

引用

页码：1443 / 1446

页数：4

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