A Sir2-Like Protein Participates in Mycobacterial NHEJ

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A Sir2-Like Protein Participates in Mycobacterial NHEJ. / Li, Z; Wen, Jikai; Lin, Y; Wang, S; Xue, P; Zhang, Z; Zhou, Y; Wang, X; Sui, L; Bi, LJ; Zhang, XE.

In: PLoS ONE, Vol. 6, No. 5, 01.05.2011, p. e20045.

Research output: Contribution to journalArticle

Harvard

Li, Z, Wen, J, Lin, Y, Wang, S, Xue, P, Zhang, Z, Zhou, Y, Wang, X, Sui, L, Bi, LJ & Zhang, XE 2011, 'A Sir2-Like Protein Participates in Mycobacterial NHEJ', PLoS ONE, vol. 6, no. 5, pp. e20045. https://doi.org/10.1371/journal.pone.0020045

APA

Li, Z., Wen, J., Lin, Y., Wang, S., Xue, P., Zhang, Z., Zhou, Y., Wang, X., Sui, L., Bi, LJ., & Zhang, XE. (2011). A Sir2-Like Protein Participates in Mycobacterial NHEJ. PLoS ONE, 6(5), e20045. https://doi.org/10.1371/journal.pone.0020045

Vancouver

Author

Li, Z ; Wen, Jikai ; Lin, Y ; Wang, S ; Xue, P ; Zhang, Z ; Zhou, Y ; Wang, X ; Sui, L ; Bi, LJ ; Zhang, XE. / A Sir2-Like Protein Participates in Mycobacterial NHEJ. In: PLoS ONE. 2011 ; Vol. 6, No. 5. pp. e20045.

Bibtex

@article{d6f7133cb0694a9b9b437cec207c15fc,
title = "A Sir2-Like Protein Participates in Mycobacterial NHEJ",
abstract = "In eukaryotic cells, repair of DNA double-strand breaks (DSBs) by the nonhomologous end-joining (NHEJ) pathway is critical for genome stability. In contrast to the complex eukaryotic repair system, bacterial NHEJ apparatus consists of only two proteins, Ku and a multifunctional DNA ligase (LigD), whose functional mechanism has not been fully clarified. We show here for the first time that Sir2 is involved in the mycobacterial NHEJ repair pathway. Here, using tandem affinity purification (TAP) screening, we have identified an NAD-dependent deacetylase in mycobacteria which is a homologue of the eukaryotic Sir2 protein and interacts directly with Ku. Results from an in vitro glutathione S-transferase (GST) pull-down assay suggest that Sir2 interacts directly with LigD. Plasmid-based end-joining assays revealed that the efficiency of DSB repair in a sir2 deletion mutant was reduced 2-fold. Moreover, the Delta sir2 strain was about 10-fold more sensitive to ionizing radiation (IR) in the stationary phase than the wild-type. Our results suggest that Sir2 may function closely together with Ku and LigD in the nonhomologous end-joining pathway in mycobacteria.",
author = "Z Li and Jikai Wen and Y Lin and S Wang and P Xue and Z Zhang and Y Zhou and X Wang and L Sui and LJ Bi and XE Zhang",
year = "2011",
month = may,
day = "1",
doi = "10.1371/journal.pone.0020045",
language = "English",
volume = "6",
pages = "e20045",
journal = "PLoSONE",
issn = "1932-6203",
publisher = "Public Library of Science (PLOS)",
number = "5",

}

RIS

TY - JOUR

T1 - A Sir2-Like Protein Participates in Mycobacterial NHEJ

AU - Li, Z

AU - Wen, Jikai

AU - Lin, Y

AU - Wang, S

AU - Xue, P

AU - Zhang, Z

AU - Zhou, Y

AU - Wang, X

AU - Sui, L

AU - Bi, LJ

AU - Zhang, XE

PY - 2011/5/1

Y1 - 2011/5/1

N2 - In eukaryotic cells, repair of DNA double-strand breaks (DSBs) by the nonhomologous end-joining (NHEJ) pathway is critical for genome stability. In contrast to the complex eukaryotic repair system, bacterial NHEJ apparatus consists of only two proteins, Ku and a multifunctional DNA ligase (LigD), whose functional mechanism has not been fully clarified. We show here for the first time that Sir2 is involved in the mycobacterial NHEJ repair pathway. Here, using tandem affinity purification (TAP) screening, we have identified an NAD-dependent deacetylase in mycobacteria which is a homologue of the eukaryotic Sir2 protein and interacts directly with Ku. Results from an in vitro glutathione S-transferase (GST) pull-down assay suggest that Sir2 interacts directly with LigD. Plasmid-based end-joining assays revealed that the efficiency of DSB repair in a sir2 deletion mutant was reduced 2-fold. Moreover, the Delta sir2 strain was about 10-fold more sensitive to ionizing radiation (IR) in the stationary phase than the wild-type. Our results suggest that Sir2 may function closely together with Ku and LigD in the nonhomologous end-joining pathway in mycobacteria.

AB - In eukaryotic cells, repair of DNA double-strand breaks (DSBs) by the nonhomologous end-joining (NHEJ) pathway is critical for genome stability. In contrast to the complex eukaryotic repair system, bacterial NHEJ apparatus consists of only two proteins, Ku and a multifunctional DNA ligase (LigD), whose functional mechanism has not been fully clarified. We show here for the first time that Sir2 is involved in the mycobacterial NHEJ repair pathway. Here, using tandem affinity purification (TAP) screening, we have identified an NAD-dependent deacetylase in mycobacteria which is a homologue of the eukaryotic Sir2 protein and interacts directly with Ku. Results from an in vitro glutathione S-transferase (GST) pull-down assay suggest that Sir2 interacts directly with LigD. Plasmid-based end-joining assays revealed that the efficiency of DSB repair in a sir2 deletion mutant was reduced 2-fold. Moreover, the Delta sir2 strain was about 10-fold more sensitive to ionizing radiation (IR) in the stationary phase than the wild-type. Our results suggest that Sir2 may function closely together with Ku and LigD in the nonhomologous end-joining pathway in mycobacteria.

U2 - 10.1371/journal.pone.0020045

DO - 10.1371/journal.pone.0020045

M3 - Article

C2 - 21637345

VL - 6

SP - e20045

JO - PLoSONE

JF - PLoSONE

SN - 1932-6203

IS - 5

ER -