Premium
A reversible acetylation system in mycobacteria
Author(s) -
Xu Hua,
Hegde Subray,
Blanchard John S.
Publication year - 2012
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.26.1_supplement.803.1
Subject(s) - acetylation , acetyltransferase , sirtuin , lysine , biochemistry , sirt2 , acetyltransferases , chemistry , acetyl coa , mycobacterium smegmatis , sirtuin 1 , nad+ kinase , biology , mycobacterium tuberculosis , enzyme , amino acid , gene , medicine , tuberculosis , downregulation and upregulation , pathology
Recent proteomics studies have revealed that protein acetylation is an abundant and evolutionarily conserved post‐translational modification from prokaryotes to eukaryotes. Although an astonishing number of acetylated proteins have been identified, the acetyltransferases that target these proteins remain largely unknown. Here we characterized a reversible acetylation system in Mycobacterium smegmatis, which includes MSMEG_5458 and MSMEG_5175. We show that MSMEG_5458 is a protein acetyltransferase ( Ms Pat) that specifically acetylates the ε‐amino group of a highly conserved lysine residue in acetyl‐CoA synthetase (ACS). This acetylation results in the inactivation of ACS activity. Interestingly, acetylation by Ms Pat is dependent on 3′,5′‐cyclic adenosine monophosphate (cAMP), indicating that Ms Pat is a downstream target of the intracellular cAMP signaling pathway. In addition, we show that MSMEG_5175, a sirtuin‐like deacetylase, as well as its orthologue in M. tuberculosis Rv1151c, reactivates acetylated ACS through an NAD + ‐dependent deacetylation. Therefore, Pat and the sirtuin‐like deacetylase in mycobacteria constitute a reversible acetylation system that regulates the activity of ACS. Currently we are searching for other targets of this system.