Article published in Nature Communications

In this publication, lead by Prof. Michael Lammers from our Institute of Biochemistry – we show, based on crystal structures and AlphaFold2 predictions that the AcuA•AcsA complex (Bacillus subtilis acetyltransferase AcuA and AMP-forming acetyl-CoA synthetase AcsA) dissociates upon acetyl-CoA dependent acetylation of AcsA by AcuA. Moreover, we provide mechanistic insights into the regulation of AMP-forming acetyl-CoA synthetases by lysine acetylation which enabled to discovere an intrinsic phosphotransacetylase allowing modulation of its activity based on AcP and CoA levels, see here.