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Verfasst von:Noort, Vera van [VerfasserIn]   i
 Vonkova, Ivana [VerfasserIn]   i
 Betts, Matthew J. [VerfasserIn]   i
 Russell, Robert B. [VerfasserIn]   i
 Bork, Peer [VerfasserIn]   i
 Gavin, Anne-Claude [VerfasserIn]   i
Titel:Cross-talk between phosphorylation and lysine acetylation in a genome-reduced bacterium
Verf.angabe: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
E-Jahr:2012
Jahr:2012 Feb 28
Umfang:16 S.
Fussnoten:Gesehen am 23.10.2018
Titel Quelle:Enthalten in: Molecular systems biology
Ort Quelle:[London] : Nature Publishing Group UK, 2005
Jahr Quelle:2012
Band/Heft Quelle:8(2012), Artikel-ID 571
ISSN Quelle:1744-4292
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.
DOI:doi:10.1038/msb.2012.4
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kostenfrei: Volltext: http://dx.doi.org/10.1038/msb.2012.4
 kostenfrei: Volltext: https://www.embopress.org/doi/full/10.1038/msb.2012.4
 DOI: https://doi.org/10.1038/msb.2012.4
Datenträger:Online-Ressource
Sprache:eng
K10plus-PPN:1582200343
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