Structural and functional characterization of the bacterial biofilm activator RemA.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 34588455.
- Also identified by DOI 10.1038/s41467-021-26005-4 and PMC identifier 8481266.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
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.
Medical subject headings
- Bacterial Proteins
- Biofilms
- DNA, Bacterial
- Geobacillus
- Transcription Factors