Cross‐talk between phosphorylation and lysine acetylation in a genome‐reduced bacterium

• DOI: 10.1038/msb.2012.4
• Publication Date: 2012-02-28T14:27:47Z
• Authors: Vera van Noort; Jan Seebacher; Samuel Bader; Shabaz Mohammed; Ivana Vonkova; Matthew J Betts; Sebastian Kühner; Runjun Kumar; Tobias Maier; Martina O'Flaherty; Vladimir Rybin; Arne Schmeisky; Eva Yus; Jörg Stülke; Luis Serrano; Robert B Russell; Albert JR Heck; Peer Bork; Anne‐Claude Gavin
• Keywords: Medicine (General); Proteome; kinase; QH301-705.5; post‐translational modification; Microbiologia; Proteòmica; Models, Biological; Article; phosphatase; Evolution, Molecular; 03 medical and health sciences; R5-920; Genome Size; Catalytic Domain; Pneumonia, Mycoplasma; Gene Regulatory Networks; Biology (General); Phosphorylation; 0303 health sciences; Organisms, Genetically Modified; Lysine; Acetylation; 3. Good health; network; Acetylesterase; N‐acetyltransferase; Protein Kinases; Protein Processing, Post-Translational; Genome, Bacterial; Metabolic Networks and Pathways

Protein 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.