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Published on: November 12, 2012
Comparative functional analysis of the RcsC sensor kinase from different Enterobacteriaceae
Ya-Hui Huang1, Lionel Ferrières, David J Clarke
1Department of Biology and Biochemistry, University of Bath, Bath, UK.
FEMS Microbiology Letters
|March 6, 2009
Summary
The Rcs phosphorelay is conserved in Enterobacteriaceae. While RcsC homologues from E. coli, Salmonella, and Yersinia activate the pathway, only E. coli and Salmonella RcsC restored biofilm formation in E. coli K-12.
Area of Science:
- Microbiology
- Molecular Biology
- Bacterial Genetics
Background:
- The Rcs phosphorelay is a crucial signaling pathway in Enterobacteriaceae.
- It comprises RcsC (sensor kinase), RcsD (HPt protein), and RcsB (response regulator).
- Functional conservation of RcsC homologues across enteric bacteria is not fully understood.
Purpose of the Study:
- To investigate the functional conservation of RcsC homologues from pathogenic bacteria.
- To assess the ability of E. coli, Salmonella enterica, and Yersinia pestis RcsC to complement an E. coli K-12 rcsC mutation.
Main Methods:
- Complementation assays in an E. coli K-12 rcsC mutant.
- Measurement of cpsB-lacZ expression upon DjlA overproduction (RcsC activation signal).
- Assessment of biofilm formation restoration.
Main Results:
- All tested RcsC homologues (E. coli, S. enterica, Y. pestis) increased cpsB-lacZ expression in response to DjlA.
- This indicates conserved signal sensing and transduction capabilities.
- Y. pestis RcsC failed to restore normal biofilm formation, linked to increased kinase activity.
Conclusions:
- The core signaling domains of RcsC are functionally conserved across Enterobacteriaceae.
- Differences in RcsC kinase activity can impact downstream functions like biofilm formation.
- Functional divergence exists despite core pathway conservation.
