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In Streptomyces lividans , acetyl‐CoA synthetase activity is controlled by O‐ serine and N ɛ ‐ lysine acetylation
Author(s) -
VanDrisse Chelsey M.,
EscalanteSemerena Jorge C.
Publication year - 2018
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/mmi.13901
Subject(s) - acetylation , acetyltransferase , acetyltransferases , biology , biochemistry , lysine , enzyme , acetyl coa , streptomyces , sirtuin , nad+ kinase , amino acid , bacteria , gene , genetics
Summary Protein acetylation is a rapid mechanism for control of protein function. Acetyl‐CoA synthetase (AMP‐forming, Acs) is the paradigm for the control of metabolic enzymes by lysine acetylation. In many bacteria, type I or II protein acetyltransferases acetylate Acs, however, in actinomycetes type III protein acetyltransferases control the activity of Acs. We measured changes in the activity of the Streptomyces lividans Acs ( Sl Acs) enzyme upon acetylation by PatB using in vitro and in vivo analyses. In addition to the acetylation of residue K610, residue S608 within the acetylation motif of Sl Acs was also acetylated (PKTRSGK 610 ). S608 acetylation rendered Sl Acs inactive and non‐acetylatable by PatB. It is unclear whether acetylation of S608 is enzymatic, but it was clear that this modification occurred in vivo in Streptomyces . In S. lividans , an NAD + ‐dependent sirtuin deacetylase from Streptomyces , SrtA (a homologue of the human SIRT4 protein) was needed to maintain Sl Acs function in vivo . We have characterized a sirtuin‐dependent reversible lysine acetylation system in Streptomyces lividans that targets and controls the Acs enzyme of this bacterium. These studies raise questions about acetyltransferase specificity, and describe the first Acs enzyme in any organism whose activity is modulated by O‐ Ser and N ɛ ‐ Lys acetylation.