Journal
FEMS MICROBIOLOGY LETTERS
Volume 340, Issue 1, Pages 19-23Publisher
WILEY-BLACKWELL
DOI: 10.1111/1574-6968.12067
Keywords
Streptococcus pneumoniae; MurC; StkP; PhpP; kinase; phosphatase
Categories
Funding
- NIAID NIH HHS [5R03-AI081005] Funding Source: Medline
Ask authors/readers for more resources
Streptococcus pneumoniae contains a single Ser/Thr kinase-phosphatase pair known as StkP-PhpP. Here, we report the interaction of StkP-PhpP with S.pneumoniae UDP-N-acetylmuramoyl:L-alanine ligase, MurC, an enzyme that synthesizes an essential intermediate of the cell wall peptidoglycan pathway. Combinatorial phage display using StkP as target selected the peptide sequence YEVCGSDTVGC as an interacting partner and subsequently confirmed by ELISA. The phage peptide sequence YEVCGSDTVGC aligns closely with the MurC motif spanning S.pneumoniae amino acid coordinates 3137. We show that MurC is phosphorylated by StkP and that phosphoMurC is dephosphorylated by PhpP. These data suggest a link between StkP-PhpP with the coordinated regulation of cell wall biosynthesis via MurC.
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