RsaM: a unique dominant regulator of AHL quorum sensing in bacteria

Microbiology (Reading). 2023 Nov;169(11):001417. doi: 10.1099/mic.0.001417.

Abstract

Quorum sensing (QS) in proteobacteria is a mechanism to control gene expression orchestrated by the LuxI/LuxR protein family pair, which produces and responds to N-acyl homoserine lactone (AHL) diffusible signal molecules. QS is often regarded as a cell density response via the sensing of/response to the concentrations of AHLs, which are constantly basally produced by bacterial cells. The luxI/R systems, however, undergo supra-regulation in response to external stimuli and many regulators have been implicated in controlling QS in bacteria, although it remains unclear how most of these regulators and cues contribute to the QS response. One regulator, called RsaM, has been reported in a few proteobacterial species to have a stringent role in the control of AHL QS. RsaMs are small, in the range of 140-170 aa long, and are found in several genera, principally in Burkholderia and Acinetobacter. The gene encoding RsaM is always located as an independent transcriptional unit, situated adjacent to QS luxI and/or luxR loci. One of the most remarkable aspects of RsaM is its uniqueness; it does not fall into any of the known bacterial regulatory families and it possesses a distinct and novel fold that does not exhibit binding affinity for nucleic acids or AHLs. RsaM stands out as a distinctive regulator in bacteria, as it is likely to have an important ecological role, as well as unravelling a novel way of gene regulation in bacteria.

Keywords: AHL; LuxI/R; RsaM; bacteria; quorum sensing; regulation.

MeSH terms

  • Acyl-Butyrolactones* / metabolism
  • Bacteria / genetics
  • Bacteria / metabolism
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Gene Expression Regulation, Bacterial
  • Quorum Sensing* / genetics
  • Trans-Activators / genetics
  • Trans-Activators / metabolism

Substances

  • Acyl-Butyrolactones
  • Trans-Activators
  • Bacterial Proteins