Structural and functional characterization of the bacterial biofilm activator RemA

• DOI: 10.1038/s41467-021-26005-4
• Publication Date: 2021-09-29T10:21:04Z
• Authors: Tamara Hoffmann; Devid Mrusek; Patricia Bedrunka; Fabiana Burchert; Christopher-Nils ...; Daniel B. Kearns; Florian Altegoer; Erhard Bremer; Gert Bange
• Keywords: DNA, Bacterial; 0301 basic medicine; Models, Genetic; Science; Q; Geobacillus; Gene Expression Regulation, Bacterial; Regulatory Sequences, Nucleic Acid; Crystallography, X-Ray; Article; Recombinant Proteins; 03 medical and health sciences; Bacterial Proteins; Biofilms; Mutagenesis, Site-Directed; Protein Interaction Domains and Motifs; Protein Multimerization; Bacillus subtilis; Transcription Factors

AbstractBacillus 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.