【摘 要】
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Reversible lysinc acetylation (RLA) is used by cells of all domains of life to modulate protein function.To date, bacterial acetylation/deacetylation systems have been studied in a few bacteria (e.g.,
【出 处】
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2015年上海市研究生学术论坛(生物化工)
论文部分内容阅读
Reversible lysinc acetylation (RLA) is used by cells of all domains of life to modulate protein function.To date, bacterial acetylation/deacetylation systems have been studied in a few bacteria (e.g.,Salmonella enterica, Bacillus subtilis, Escherichia coli, Erwinia amylovora,Mycobacterium tuberculosis, and Geobacillus kaustophilus), but little is known about RLA in antibiotic-producing actinomycetes.Here, we identify the Gcn5-1ike protein acetyltransferase AcuA of Saccharopolyspora erythraea(SacAcuA, SACE_5148) as the enzyme responsible for the acetylation of the AMP-forming acetyl coenzyme A synthetase (SacAcsA, SACE_2375).Acetylated SacAcsA was deacetylated by a sirtuin-type NAD-dependent consuming deacetylase(SacSrtN,SACE_3798).In vitro acetylation/deacetylation of SacAcsA enzyme was studied by Western blotting,and acetylationof lysine residues Lys237, Lys380, Lys611, and Lys628 was confirmed by mass spectrometry.In a strain devoid of SacAcuA, none of the above-mentioned Lys residues of SacAcsA was acetylated.To our knowledge, the ability of SacAcuA to acetylate multiple Lys residues is unique among AcuA-type acetyltransferases.Results from site-specific mutagenesis experiments showed that the activity of SacAcsA was controlled by lysine acetylation.Lastly,immunoprecipitation data showed that in vivo acetylation of SacAcsA was influenced by glucose and acetate availability.These results suggested that reversible acetylation may also be a conserved regulatory posttranslational modification strategy in antibiotic-producing actinomycetes.
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