The E. coli sirtuin CobB shows no preference for enzymatic and nonenzymatic lysine acetylation substrate sites
Alaa AbouElfetouh, Misty L. Kuhn, Linda I. Hu, Michael D. Scholle, Dylan J. Sorensen, Alexandria K. Sahu, Dörte Becher, Haike Antelmann, Milan Mrksich, Wayne F. Anderson, Bradford W. Gibson, Birgit Schilling and Alan J. Wolfe
Article first published online: 22 NOV 2014 | DOI: 10.1002/mbo3.223
We provide genetic, mass spectrometric, structural, and immunological evidence that CobB, a member of the sirtuin family of protein deacetylases, can reverse acetylation regardless of acetyl donor or acetylation mechanism. We also provide evidence that CobB is the predominant or perhaps the sole deacetylase in E. coli. Finally, we present evidence that three-dimensional structure should be used to predict CobB substrates.