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

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 P(eps) 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.

journal_name

Mol Microbiol

journal_title

Molecular microbiology

authors

Winkelman JT,Bree AC,Bate AR,Eichenberger P,Gourse RL,Kearns DB

doi

10.1111/mmi.12235

subject

Has Abstract

pub_date

2013-06-01 00:00:00

pages

984-97

issue

5

eissn

0950-382X

issn

1365-2958

journal_volume

88

pub_type

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