SIRT7 promotes genome integrity and modulates non‐homologous end joining DNA repair

Abstract

Sirtuins, a family of protein deacetylases, promote cellular homeostasis by mediating communication between cells and environment. The enzymatic activity of the mammalian sirtuin SIRT7 targets acetylated lysine in the N‐terminal tail of histone H3 (H3K18Ac), thus modulating chromatin structure and transcriptional competency. SIRT7 deletion is associated with reduced lifespan in mice through unknown mechanisms. Here, we show that SirT7‐knockout mice suffer from partial embryonic lethality and a progeroid‐like phenotype. Consistently, SIRT7‐deficient cells display increased replication stress and impaired DNA repair. SIRT7 is recruited in a PARP1‐dependent manner to sites of DNA damage, where it modulates H3K18Ac levels. H3K18Ac in turn affects recruitment of the damage response factor 53BP1 to DNA double‐strand breaks (DSBs), thereby influencing the efficiency of non‐homologous end joining (NHEJ). These results reveal a direct role for SIRT7 in DSB repair and establish a functional link between SIRT7‐mediated H3K18 deacetylation and the maintenance of genome integrity.

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    SIRT7 promotes genome integrity and modulates non‐homologous end joining DNA repair · 2016

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Cited by papers we hold 4

• SIRT7 antagonizes human stem cell aging as a heterochromatin stabilizer · 2020
  No notice
• The Roles of Histone Deacetylases and Their Inhibitors in Cancer Therapy · 2020
  No notice
• SIRT7 antagonizes TGF-β signaling and inhibits breast cancer metastasis · 2017
  No notice
• Sirtuins in metabolism, DNA repair and cancer · 2016
  No notice

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