期刊
FEMS MICROBIOLOGY LETTERS
卷 340, 期 1, 页码 19-23出版社
WILEY-BLACKWELL
DOI: 10.1111/1574-6968.12067
关键词
Streptococcus pneumoniae; MurC; StkP; PhpP; kinase; phosphatase
类别
资金
- NIAID NIH HHS [5R03-AI081005] Funding Source: Medline
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.
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