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

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dc.contributor.author Noort, Vera van
dc.contributor.author Seebacher, Jan
dc.contributor.author Bader, Samuel
dc.contributor.author Mohammed, Shabaz
dc.contributor.author Vonkova, Ivana
dc.contributor.author Betts, Matthew J.
dc.contributor.author Kühner, Sebastian
dc.contributor.author Kumar, Runjun
dc.contributor.author Maier, Tobias
dc.contributor.author O'Flaherty, Martina
dc.contributor.author Rybin, Vladimir
dc.contributor.author Schmeisky, Arne
dc.contributor.author Yus, Eva
dc.contributor.author Stülke, Jörg
dc.contributor.author Serrano Pubull, Luis, 1982-
dc.contributor.author Russell, Robert B.
dc.contributor.author Heck, Albert J.R.
dc.contributor.author Bork, Peer
dc.contributor.author Gavin, Anne-Claude
dc.date.accessioned 2014-04-29T08:44:34Z
dc.date.available 2014-04-29T08:44:34Z
dc.date.issued 2012
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.2012.4
dc.identifier.issn 1744-4292
dc.identifier.uri http://hdl.handle.net/10230/22228
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/pdf
dc.language.iso eng
dc.publisher Nature Publishing Group
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 License
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 bacterium
dc.type info:eu-repo/semantics/article
dc.identifier.doi http://dx.doi.org/10.1038/msb.2012.4
dc.rights.accessRights info:eu-repo/semantics/openAccess
dc.type.version info:eu-repo/semantics/publishedVersion

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