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

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 pho

SUBMITTER: van Noort V 

PROVIDER: S-EPMC3293634 | biostudies-literature | 2012 Feb

REPOSITORIES: biostudies-literature