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

Journal article

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.

Authors: van Noort, V; Seebacher, J; Bader, S; Mohammed, S; Vonkova, I

• Publication status: Published
• Peer review status: Peer reviewed
• Publisher: EMBO Press
• Journal: Molecular systems biology
• Volume: 8
• Pages: 571
• Publication date: 2012-02-01
• DOI: 10.1038/msb.2012.4
• EISSN: 1744-4292
• ISSN: 1744-4292
• Language: English
• Keywords: Evolution, Molecular; Proteome; Lysine; Metabolic Networks and Pathways; Acetylation; Pneumonia, Mycoplasma; Genome Size; Protein Processing, Post-Translational; Phosphorylation; Organisms, Genetically Modified; Catalytic Domain; Models, Biological; Genome, Bacterial; Gene Regulatory Networks; Acetylesterase; Protein Kinases