Premium
RemA is a DNA ‐binding protein that activates biofilm matrix gene expression in B acillus subtilis
Author(s) -
Winkelman Jared T.,
Bree Anna C.,
Bate Ashley R.,
Eichenberger Patrick,
Gourse Richard L.,
Kearns Daniel B.
Publication year - 2013
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/mmi.12235
Subject(s) - operon , bacillus subtilis , biology , promoter , biofilm , gene , activator (genetics) , dna , regulation of gene expression , lac operon , gene expression , transcriptional regulation , microbiology and biotechnology , biochemistry , genetics , bacteria , mutant
Summary Biofilm formation in B acillus 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 r egulator of the e xtracellular m atrix genes, but it also activated genes involved in osmoprotection, leading to the identification of another direct target, the opuA operon.