Escherichia coli YmdB regulates biofilm formation independently of its role as an RNase III modulator

Abstract

BackgroundRibonuclease III (RNase III) activity modulates hundreds of genes in Escherichia coli (E. coli). YmdB, a member of the macrodomain protein family, is one of known trans-acting regulators of RNase III activity; however, the significance of its regulatory role in specific bacterial cellular processes and related genes has not been determined. YmdB overexpression was used to model YmdB-induced RNase III inhibition in vivo, and microarray analysis identified gene targets and cellular processes related to RNase III inhibition.ResultsThe expression of >2,000 E. coli genes was modulated by YmdB induction; 129 genes were strongly regulated, of which 80 have not been reported as RNase III targets. Of these, ten are involved in biofilm formation. Significantly, YmdB overexpression also inhibited biofilm formation via a process that is not uniquely dependent upon RNase III inhibition. Moreover, biofilm formation is interdependently regulated by RpoS, a known stress response regulator and biofilm inhibitor, and by YmdB.ConclusionsThis is the first global profile of target genes modulated by YmdB-induced RNase III inhibition in E. coli, and the data reveal a novel, hitherto unrecognized regulatory role for YmdB in biofilm modulation.

Disruption of Macrodomain Protein SCO6735 Increases Antibiotic Production in Streptomyces coelicolor

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“…Subsequently, YmdB interacts with the ribonuclease RNase III and acts as a negative regulator of its cleavage activity (Kim et al 2008;Paudyal et al 2015). Furthermore, YmdB was suggested as a regulator of gene expression both through RNase III regulation as well as in an RNase III-independent manner, thereby influencing biofilm formation and antimicrobial resistance (Kim et al 2013(Kim et al , 2017. While it was shown that YmdB is catalytically active Zhang et al 2015b), the role of this activity in vivo remains elusive.…”

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