ArticleNature communications2021
Structural and functional characterization of the bacterial biofilm activator RemA.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed, 6 citations in OpenAlex.
- Molecular insights into the promiscuous ApThe Journal of biological chemistry · 2026Article
- MeeY and YybP, two proteins regulated by manganese-sensing riboswitches, are required for Bacillus subtilis biofilm formation.NPJ biofilms and microbiomes · 2026Article
- The bacterial swarming factor SwrD forms hexameric rings reminiscent of DNA-binding proteins.bioRxiv : the preprint server for biology · 2026Article
- Amalgamation of Biofilms and Synthetic Biology: A Paradigm Shift in Biotechnology.Medical principles and practice : international journal of the Kuwait University, Health Science Centre · 2026Review
- A model industrial workhorse: Bacillus subtilis strain 168 and its genome after a quarter of a century.Microbial biotechnology · 2023Review
- Influence ofFrontiers in microbiology · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.