Noort, Vera vanSeebacher, JanBader, SamuelMohammed, ShabazVonkova, IvanaBetts, Matthew J.Kühner, SebastianKumar, RunjunMaier, TobiasO'Flaherty, MartinaRybin, VladimirSchmeisky, ArneYus, EvaStülke, JörgSerrano Pubull, Luis, 1982-Russell, Robert B.Heck, Albert J.R.Bork, PeerGavin, Anne-Claude2014-04-292014-04-292012van Noort V, Seebacher J, Bader S, Mohammed S, Vonkova I, Betts MJ et al. Cross-talk between phosphorylation and lysine acetylation in a genome-reduced bacterium. Mol Syst Biol. 2012; 8: 571. DOI: 10.1038/msb.2012.41744-4292http://hdl.handle.net/10230/22228Protein post-translational modifications (PTMs) represent important regulatory states that when combined have been hypothesized to act as molecular codes and to generate a functional diversity beyond genome and transcriptome. We systematically investigate the interplay of protein phosphorylation with other post-transcriptional regulatory mechanisms in the genome-reduced bacterium Mycoplasma pneumoniae. Systematic perturbations by deletion of its only two protein kinases and its unique protein phosphatase identified not only the protein-specific effect on the phosphorylation network, but also a modulation of proteome abundance and lysine acetylation patterns, mostly in the absence of transcriptional changes. Reciprocally, deletion of the two putative N-acetyltransferases affects protein phosphorylation, confirming cross-talk between the two PTMs. The measured M. pneumoniae phosphoproteome and lysine acetylome revealed that both PTMs are very common, that (as in Eukaryotes) they often co-occur within the same protein and that they are frequently observed at interaction interfaces and in multifunctional proteins. The results imply previously unreported hidden layers of post-transcriptional regulation intertwining phosphorylation with lysine acetylation and other mechanisms that define the functional state of a cell.application/pdfengThis is an open-access article distributed under the terms of the Creative Commons Attribution Non-Commercial Share Alike LicenseProteòmicaMicrobiologiainfo:eu-repo/semantics/articlehttp://dx.doi.org/10.1038/msb.2012.4info:eu-repo/semantics/openAccess