Albert Jr Heck

Publications (2)8.63 Total impact

• Source

  Available from: Robert B Russell

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

  Vera van Noort, Jan Seebacher, Samuel Bader, Shabaz Mohammed, Ivana Vonkova, Matthew J Betts, Sebastian K|[uuml]|hner, Runjun Kumar, Tobias Maier, Martina O'Flaherty, Vladimir Rybin, Arne Schmeisky, Eva Yus, J|[ouml]|rg St|[uuml]|lke, Luis Serrano, Robert B Russell, Albert JR Heck, Peer Bork, Anne-Claude Gavin
  [show abstract] [hide abstract]
  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.
  Molecular Systems Biology. 02/2012; 8(1).
• Source

  Available from: Vera van Noort

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

  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 J R Heck, Peer Bork, Anne-Claude Gavin
  [show abstract] [hide abstract]
  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.
  Molecular Systems Biology 01/2012; 8:571. · 8.63 Impact Factor