Phosphorylation of the Streptococcus pneumoniae cell wall biosynthesis enzyme MurC by a eukaryotic-like Ser/Thr kinase

Abstract 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 pat...

Full description

Saved in:
Bibliographic Details
Published in:FEMS microbiology letters 2013-03, Vol.340 (1), p.19-23
Main Authors: Falk, Shaun P., Weisblum, Bernard
Format: Article
Language:English
Subjects:
Amino acids
Bacterial Proteins - metabolism
Bacteriology
Binding Sites
Biological and medical sciences
Biosynthesis
Cell Surface Display Techniques
Enzyme-Linked Immunosorbent Assay
Fundamental and applied biological sciences. Psychology
kinase
Microbiology
Miscellaneous
MurC
Peptide Synthases - metabolism
phosphatase
Phosphorylation
PhpP
Protein Processing, Post-Translational
Protein-Serine-Threonine Kinases - metabolism
StkP
Streptococcus pneumoniae
Streptococcus pneumoniae - pathogenicity
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Abstract 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 31–37. 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.
ISSN:0378-1097
1574-6968
DOI:10.1111/1574-6968.12067