Discovery and characterization of Ku acetylation in Mycobacterium smegmatis

FEMS Microbiology Letters
Ying ZhouLi-Jun Bi

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.

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Citations

Sep 22, 2015·Proteomics·Tassadit OuidirJulie Hardouin
Apr 26, 2017·Journal of Bacteriology·Valerie J Carabetta, Ileana M Cristea
Sep 27, 2018·Journal of Bacteriology·Arunima MishraHansel M Fletcher
Dec 6, 2018·Nucleic Acids Research·Pierre DupuyClaude Bruand
Feb 13, 2019·Molecular Microbiology·Claire BertrandPierre Leblond
Jan 1, 2017·Acta Biochimica Et Biophysica Sinica·Jing GuJiaoyu Deng
May 1, 2020·Frontiers in Microbiology·Monika Pióro, Dagmara Jakimowicz

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