RemA is a DNA-binding protein that activates biofilm matrix gene expression in Bacillus subtilis

Jared T. Winkelman, Anna C. Bree, Ashley R. Bate, Patrick Eichenberger, Richard L. Gourse, Daniel B. Kearns

Research output: Contribution to journalArticle

Abstract

Biofilm formation in Bacillus subtilis requires expression of the eps and tapA-sipW-tasA operons to synthesize the extracellular matrix components, extracellular polysaccharide and TasA amyloid proteins, respectively. Expression of both operons is inhibited by the DNA-binding protein master regulator of biofilm formation SinR and activated by the protein RemA. Here we show that RemA is a DNA-binding protein that binds to multiple sites upstream of the promoters of both operons and is both necessary and sufficient for transcriptional activation in vivo and in vitro. We further show that SinR negatively regulates eps operon expression by occluding RemA binding and thus for the Peps promoter SinR functions as an anti-activator. Finally, transcriptional profiling indicated that RemA was primarily a regulator of the extracellular matrix genes, but it also activated genes involved in osmoprotection, leading to the identification of another direct target, the opuA operon.

Original languageEnglish (US)
Pages (from-to)984-997
Number of pages14
JournalMolecular Microbiology
Volume88
Issue number5
DOIs
StatePublished - Jun 1 2013

    Fingerprint

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology

Cite this