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Reversible lysine acetylation (RLA) is a widespread regulatory mechanism that modulates the function of proteins involved in diverse cellular processes. A strong case has been made for RLA control exerted by homologues of the  Salmonella enterica  protein acetyltransferase ( Se Pat) enzyme on the broadly distributed AMP-forming CoA ligase (a.k.a. acyl-CoA synthetases) family of metabolic enzymes, with acetyl-CoA synthetase (Acs) being the paradigm in the field. Here we investigate why the Acs homologue in  Streptomyces lividans  ( Sl Acs) is poorly acetylated  in vitro  by the  S. lividans  protein acetyltransferase ( Sl Pat) enzyme. Chimeras of  S. enterica  Acs ( Se Acs) and  S. lividans  Acs ( Sl Acs) constructed during the course of this work were acetylated by  Sl PatA  in vitro , retained most of their activity, and were under RLA control in a heterologous host. We identified  Se Acs residues  N - and  C -terminal to the target lysine that when introduced into  Sl Acs, rendered the latter under RLA control. These results lend further support to the idea that Pat enzymes interact with extensive surfaces of their substrates. Finally, we suggest that acetylation of  Sl Acs depends on factors or conditions other than those present in our  in vitro  system. We also discuss possible explanations why  Sl Acs is not controlled by RLA as defined in other bacterial species.

plos one

Determinants within the C-Terminal Domain of Streptomyces lividans Acetyl-CoA Synthetase that Block Acetylation of Its Active Site Lysine In Vitro by the Protein Acetyltransferase (Pat) Enzyme