Background
In Streptococcus mutans, ComCDE, a peptide-induced two-component signal transduction system, forms a closed signal transduction, and even if difunctional ComE closes this signal at its headstream to avoid its infinite amplification, it is not enough for ComE to work in a concentration-dependent manner. CslAB has a chance to regulate ComCDE by controlling extracellular competence-stimulating peptide (CSP) concentration through its processing and secretion. Objectives: To first confirm the binding properties of cslAB promoter (PcslAB) with ComE, then to uncover in vivo need of cslAB expression, and finally to unveil the role of CslAB. Materials and
Conclusions
PcslAB is partially controlled by ComCDE. CslAB is a stabilizer of ComCDE signal to ensure that ComE works in a concentration-dependent manner.
Methods
Electrophoretic mobility shift assay was used to confirm the binding properties of PcslAB with ComE. In vivo cslAB transcription was detected by β-galactosidase activity because its gene has been fused to cslAB operon, and finally the role of CslAB was reviewed.
Results
PcslAB is a weak promoter responding to ComE and its binding appears to be negative cooperative. Although PcslAB is partially controlled by ComCDE, it can respond to ComCDE regulation. Supported by the obtained molecular evidence, CslAB acts as a stabilizer of ComCDE signal on the patterns of its expression. Conclusions: PcslAB is partially controlled by ComCDE. CslAB is a stabilizer of ComCDE signal to ensure that ComE works in a concentration-dependent manner.