| Literature DB >> 21365747 |
Giulia Bernardini1, Marcella Laschi, Tommaso Serchi, Simona Arena, Chiara D'Ambrosio, Daniela Braconi, Andrea Scaloni, Annalisa Santucci.
Abstract
To investigate the phosphorylation capability of serogroup A Neisseria meningitidis (MenA) and to implement our knowledge in meningococcal biology and in bacterial post-translational modifications, cell extracts were separated by 2-DE and 51 novel phosphoproteins were revealed by the use of the highly specific Ser/Thr/Tyr-phosphorylated proteins staining by Pro-Q Diamond and identified by MALDI-ToF/MS. Our results indicate that phosphorylation in MenA is comparable to that of other bacterial species. A first functional characterization of the identified modified proteins was also given, in order to understand their role in meningococcal physiopathology.Entities:
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Year: 2011 PMID: 21365747 DOI: 10.1002/pmic.201000406
Source DB: PubMed Journal: Proteomics ISSN: 1615-9853 Impact factor: 3.984