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

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 wit...

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Hauptverfasser: Noort, Vera van (VerfasserIn) , Vonkova, Ivana (VerfasserIn) , Betts, Matthew J. (VerfasserIn) , Russell, Robert B. (VerfasserIn) , Bork, Peer (VerfasserIn) , Gavin, Anne-Claude (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: 2012 Feb 28
In: Molecular systems biology
Year: 2012, Jahrgang: 8
ISSN:1744-4292
DOI:10.1038/msb.2012.4
Online-Zugang:Verlag, kostenfrei, Volltext: http://dx.doi.org/10.1038/msb.2012.4
Verlag, kostenfrei, Volltext: https://www.embopress.org/doi/full/10.1038/msb.2012.4
Volltext
Verfasserangaben: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
Beschreibung
Zusammenfassung: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.
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Beschreibung:Online Resource
ISSN:1744-4292
DOI:10.1038/msb.2012.4