Structural and functional characterization of the bacterial biofilm activator RemA

Tamara Hoffmann, Devid Mrusek, Patricia Bedrunka, Fabiana Burchert, Christopher-Nils Mais, Daniel B. Kearns, Florian Altegoer, Erhard Bremer () and Gert Bange ()
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Tamara Hoffmann: Center for Synthetic Microbiology (SYNMIKRO) & Faculty of Biology
Devid Mrusek: Center for Synthetic Microbiology (SYNMIKRO) & Faculty of Chemistry
Patricia Bedrunka: Center for Synthetic Microbiology (SYNMIKRO) & Faculty of Chemistry
Fabiana Burchert: Center for Synthetic Microbiology (SYNMIKRO) & Faculty of Chemistry
Christopher-Nils Mais: Center for Synthetic Microbiology (SYNMIKRO) & Faculty of Chemistry
Daniel B. Kearns: Indiana University
Florian Altegoer: Center for Synthetic Microbiology (SYNMIKRO) & Faculty of Chemistry
Erhard Bremer: Center for Synthetic Microbiology (SYNMIKRO) & Faculty of Biology
Gert Bange: Center for Synthetic Microbiology (SYNMIKRO) & Faculty of Chemistry

Nature Communications, 2021, vol. 12, issue 1, 1-11

Abstract: Abstract Bacillus subtilis can form structurally complex biofilms on solid or liquid surfaces, which requires expression of genes for matrix production. The transcription of these genes is activated by regulatory protein RemA, which binds to poorly conserved, repetitive DNA regions but lacks obvious DNA-binding motifs or domains. Here, we present the structure of the RemA homologue from Geobacillus thermodenitrificans, showing a unique octameric ring with the potential to form a 16-meric superstructure. These results, together with further biochemical and in vivo characterization of B. subtilis RemA, suggests that the protein can wrap DNA around its ring-like structure through a LytTR-related domain.

Date: 2021
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-26005-4

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DOI: 10.1038/s41467-021-26005-4

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