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SIRT6 protein deacetylase interacts with MYH DNA glycosylase, APE1 endonuclease, and Rad9–Rad1–Hus1 checkpoint clamp

Overview of attention for article published in BMC Molecular Biology, June 2015
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Title
SIRT6 protein deacetylase interacts with MYH DNA glycosylase, APE1 endonuclease, and Rad9–Rad1–Hus1 checkpoint clamp
Published in
BMC Molecular Biology, June 2015
DOI 10.1186/s12867-015-0041-9
Pubmed ID
Authors

Bor-Jang Hwang, Jin, Ying Gao, Guoli Shi, Amrita Madabushi, Austin Yan, Xin Guan, Michal Zalzman, Satoshi Nakajima, Li Lan, A-Lien Lu

Abstract

SIRT6, a member of the NAD(+)-dependent histone/protein deacetylase family, regulates genomic stability, metabolism, and lifespan. MYH glycosylase and APE1 are two base excision repair (BER) enzymes involved in mutation avoidance from oxidative DNA damage. Rad9-Rad1-Hus1 (9-1-1) checkpoint clamp promotes cell cycle checkpoint signaling and DNA repair. BER is coordinated with the checkpoint machinery and requires chromatin remodeling for efficient repair. SIRT6 is involved in DNA double-strand break repair and has been implicated in BER. Here we investigate the direct physical and functional interactions between SIRT6 and BER enzymes. We show that SIRT6 interacts with and stimulates MYH glycosylase and APE1. In addition, SIRT6 interacts with the 9-1-1 checkpoint clamp. These interactions are enhanced following oxidative stress. The interdomain connector of MYH is important for interactions with SIRT6, APE1, and 9-1-1. Mutagenesis studies indicate that SIRT6, APE1, and Hus1 bind overlapping but different sequence motifs on MYH. However, there is no competition of APE1, Hus1, or SIRT6 binding to MYH. Rather, one MYH partner enhances the association of the other two partners to MYH. Moreover, APE1 and Hus1 act together to stabilize the MYH/SIRT6 complex. Within human cells, MYH and SIRT6 are efficiently recruited to confined oxidative DNA damage sites within transcriptionally active chromatin, but not within repressive chromatin. In addition, Myh foci induced by oxidative stress and Sirt6 depletion are frequently localized on mouse telomeres. Although SIRT6, APE1, and 9-1-1 bind to the interdomain connector of MYH, they do not compete for MYH association. Our findings indicate that SIRT6 forms a complex with MYH, APE1, and 9-1-1 to maintain genomic and telomeric integrity in mammalian cells.

Twitter Demographics

The data shown below were collected from the profile of 1 tweeter who shared this research output. Click here to find out more about how the information was compiled.

Mendeley readers

The data shown below were compiled from readership statistics for 28 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 28 100%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 8 29%
Student > Bachelor 5 18%
Student > Doctoral Student 4 14%
Researcher 2 7%
Student > Master 1 4%
Other 1 4%
Unknown 7 25%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 9 32%
Agricultural and Biological Sciences 5 18%
Chemistry 2 7%
Engineering 2 7%
Neuroscience 1 4%
Other 2 7%
Unknown 7 25%

Attention Score in Context

This research output has an Altmetric Attention Score of 1. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 13 June 2015.
All research outputs
#4,348,280
of 5,223,626 outputs
Outputs from BMC Molecular Biology
#123
of 148 outputs
Outputs of similar age
#145,039
of 178,144 outputs
Outputs of similar age from BMC Molecular Biology
#4
of 4 outputs
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So far Altmetric has tracked 148 research outputs from this source. They receive a mean Attention Score of 1.8. This one is in the 1st percentile – i.e., 1% of its peers scored the same or lower than it.
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