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...

Full description

Saved in:
Bibliographic Details
Main Authors: Noort, Vera van (Author) , Vonkova, Ivana (Author) , Betts, Matthew J. (Author) , Russell, Robert B. (Author) , Bork, Peer (Author) , Gavin, Anne-Claude (Author)
Format: Article (Journal)
Language:English
Published: 2012 Feb 28
In: Molecular systems biology
Year: 2012, Volume: 8
ISSN:1744-4292
DOI:10.1038/msb.2012.4
Online Access: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
Get full text
Author Notes: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
Description
Summary: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.
Item Description:Gesehen am 23.10.2018
Physical Description:Online Resource
ISSN:1744-4292
DOI:10.1038/msb.2012.4