Cross-talk between phosphorylation and lysine acetylation in a genome-reduced bacterium
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- dc.contributor.author Noort, Vera vanca
- dc.contributor.author Seebacher, Janca
- dc.contributor.author Bader, Samuelca
- dc.contributor.author Mohammed, Shabazca
- dc.contributor.author Vonkova, Ivanaca
- dc.contributor.author Betts, Matthew J.ca
- dc.contributor.author Kühner, Sebastianca
- dc.contributor.author Kumar, Runjunca
- dc.contributor.author Maier, Tobiasca
- dc.contributor.author O'Flaherty, Martinaca
- dc.contributor.author Rybin, Vladimirca
- dc.contributor.author Schmeisky, Arneca
- dc.contributor.author Yus, Evaca
- dc.contributor.author Stülke, Jörgca
- dc.contributor.author Serrano Pubull, Luis, 1982-ca
- dc.contributor.author Russell, Robert B.ca
- dc.contributor.author Heck, Albert J.R.ca
- dc.contributor.author Bork, Peerca
- dc.contributor.author Gavin, Anne-Claudeca
- dc.date.accessioned 2014-04-29T08:44:34Z
- dc.date.available 2014-04-29T08:44:34Z
- dc.date.issued 2012ca
- dc.description.abstract 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.
- dc.description.sponsorship This work was partially founded by Federal/nMinistry of Education and Research (BMBF) in the framework of the/nNational Genome Research Network (NGFN) to ACG (BMBF NGNF IG/nCellular Systems Genomics, 01GS0865)
- dc.format.mimetype application/pdfca
- dc.identifier.citation van 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.2012.4ca
- dc.identifier.doi http://dx.doi.org/10.1038/msb.2012.4
- dc.identifier.issn 1744-4292ca
- dc.identifier.uri http://hdl.handle.net/10230/22228
- dc.language.iso engca
- dc.publisher Nature Publishing Groupca
- dc.relation.ispartof Molecular Systems Biology. 2012;8:571
- dc.rights This is an open-access article distributed under the terms of the Creative Commons Attribution Non-Commercial Share Alike Licenseca
- dc.rights.accessRights info:eu-repo/semantics/openAccessca
- dc.rights.uri http://creativecommons.org/licenses/by/3.0/
- dc.subject.other Proteòmica
- dc.subject.other Microbiologia
- dc.title Cross-talk between phosphorylation and lysine acetylation in a genome-reduced bacteriumca
- dc.type info:eu-repo/semantics/articleca
- dc.type.version info:eu-repo/semantics/publishedVersionca