title: Discovery and characterization of Ku acetylation in Mycobacterium smegmatis.
abstract: Lysine acetylation is an important post-translational modification and is known to regulate many eukaryotic cellular processes. Little, however, is known about acetylated proteins in prokaryotes. Here, using immunoblotting, mass spectrometry and mutagenesis studies, we investigate the acetylation dynamics of the DNA repair protein Ku and its relationship with the deacetylase protein Sir2 and the non-homologous end joining (NHEJ) pathway in Mycobacterium smegmatis. We report that acetylation of Ku increases with growth, while NHEJ activity decreases, providing support for the hypothesis that acetylation of Ku may be involved in the DNA damage response in bacteria. Ku has multiple lysine sites. Our results indicate that K29 is an important acetylation site and that deficiency of Sir2 or mutation of K29 affects the quantity of Ku and its acetylation dynamics. Our findings expand knowledge of acetylation targets in prokaryotes and indicate a new direction for further research on bacterial DNA repair mechanisms.
authors.affiliation: Laboratory of RNA Biology, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
authors.forename: Ying
authors.initials: Y
authors.lastname: Zhou
authors.affiliation: Center for Tuberculosis Control of Guangdong Province, Guangzhou 510440, China.
authors.forename: Tao
authors.initials: T
authors.lastname: Chen
authors.affiliation: Center for Tuberculosis Control of Guangdong Province, Guangzhou 510440, China.
authors.forename: Lin
authors.initials: L
authors.lastname: Zhou
authors.affiliation: Laboratory of RNA Biology, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
authors.forename: Joy
authors.initials: J
authors.lastname: Fleming
authors.affiliation: State Key Laboratory of Virology, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan 430071, China.
authors.forename: Jiaoyu
authors.initials: J
authors.lastname: Deng
authors.affiliation: State Key Laboratory of Virology, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan 430071, China.
authors.forename: Xude
authors.initials: X
authors.lastname: Wang
authors.affiliation: Laboratory of RNA Biology, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
authors.forename: Liwei
authors.initials: L
authors.lastname: Wang
authors.affiliation: Laboratory of RNA Biology, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
authors.forename: Yingying
authors.initials: Y
authors.lastname: Wang
authors.affiliation: Laboratory of RNA Biology, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
authors.forename: Xiaoli
authors.initials: X
authors.lastname: Zhang
authors.affiliation: Laboratory of RNA Biology, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
authors.forename: Wenjing
authors.initials: W
authors.lastname: Wei
authors.affiliation: Laboratory of RNA Biology, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China blj@ibp.ac.cn.
authors.forename: Lijun
authors.initials: L
authors.lastname: Bi
mesh_terms: D000107:Acetylation; D000123:Acetyltransferases / Q000378:metabolism; D001426:Bacterial Proteins / Q000378:metabolism*; D015153:Blotting, Western; D059766:DNA End-Joining Repair; D004260:DNA Repair; D004269:DNA, Bacterial / Q000235:genetics / Q000502:physiology; D004268:DNA-Binding Proteins / Q000378:metabolism*; D008239:Lysine / Q000378:metabolism*; D013058:Mass Spectrometry; D020102:Mycobacterium smegmatis / Q000235:genetics* / Q000254:growth & development / Q000378:metabolism*; D011499:Protein Processing, Post-Translational
chemical_list: D001426:Bacterial Proteins; D004269:DNA, Bacterial; D004268:DNA-Binding Proteins; D000123:Acetyltransferases; D008239:Lysine
keywords: DNA repair; Mycobacterium smegmatis; acetylation; non-homologous end joining pathway