A Sir2-Like Protein Participates in Mycobacterial NHEJ
| Autor: | Jikai Wen, Ying Zhou, Xiao Wang, Li-Jun Bi, Shi-Hua Wang, Zhongdao Li, Xian-En Zhang, Yaning Lin, Zhi-Ping Zhang, Li Sui, Peng Xue |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2011 |
| Předmět: |
DNA Ligases
Infrared Rays Recombinant Fusion Proteins lcsh:Medicine Plasma protein binding Biology DNA-binding protein Microbiology Mycobacterium chemistry.chemical_compound Plasmid Bacterial Proteins Sirtuins Gene Knock-In Techniques RNA Messenger lcsh:Science Ku Autoantigen Tandem affinity purification chemistry.chemical_classification Recombination Genetic DNA ligase Multidisciplinary Microbial Viability lcsh:R Microbial Mutation Reproducibility of Results Bacteriology Antigens Nuclear Molecular biology Cell biology Bacterial Biochemistry Non-homologous end joining DNA-Binding Proteins enzymes and coenzymes (carbohydrates) chemistry Genetic Loci lcsh:Q DNA Research Article Protein Binding |
| Zdroj: | PLoS ONE PLoS ONE, Vol 6, Iss 5, p e20045 (2011) |
| ISSN: | 1932-6203 |
| Popis: | 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 Δsir2 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. |
| Databáze: | OpenAIRE |
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