Journal
PROTEOMICS
Volume 11, Issue 15, Pages 3002-3011Publisher
WILEY
DOI: 10.1002/pmic.201100012
Keywords
Bacteria; Mass Spectra; Microbiology; Phosphoproteomics; Protein Kinases
Funding
- Landesstifitung BW
- DFG [SFB766]
- Agence Nationale de la Recherche
- Institut National de la Recherche Agronomique
Ask authors/readers for more resources
Protein phosphorylation on serine, threonine and tyrosine is established as an important regulatory modification in bacteria. A growing number of studies employing mass spectrometry-based proteomics report large protein phosphorylation datasets, providing precise evidence for in-vivo phosphorylation that is especially suitable for functional follow-up. Here, we provide an overview of the strategies currently used in bacterial phosphoproteomics, with an emphasis on gel-free proteomics and approaches that enable global detection of phosphorylation sites in bacterial proteins. The proteomics technology has matured sufficiently to permit routine characterization of phosphoproteomes and phosphopeptides with high sensitivity; we argue that the next challenge in the field will be the large-scale detection of protein kinase and phosphatase substrates and their integration into regulatory networks of the bacterial cell.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available