Journal
CURRENT OPINION IN MICROBIOLOGY
Volume 15, Issue 3, Pages 357-363Publisher
CURRENT BIOLOGY LTD
DOI: 10.1016/j.mib.2012.05.003
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Funding
- German Research Foundation [SFB 766]
- FP7 Program PRIME-XS
- Juniorprofessoren-Programm of the Baden-Wurttemberg Stiftung
- Xunta de Galicia post-doctoral program Angeles Alvarino
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Recent advances in gel-free, mass spectrometry-based proteomics have firmly established existence of serine phosphorylation, threonine phosphorylation, tyrosine phosphorylation and lysine acetylation on many bacterial proteins. Intriguingly, numerous proteins have been shown to be modified by both modifications, leading to the emerging concept of cross-talk between posttranslational modifications in bacteria. This concept is further supported by biological follow-up studies that are starting to reveal bacterial proteins and processes regulated by multiple modifications. In this review, we provide an overview of the large-scale studies involving protein phosphorylation and acetylation in bacteria and discuss some of the current examples of cross-talk between these and other bacterial modifications.
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