ArticleJournal of molecular biology2014
A DNA mimic: the structure and mechanism of action for the anti-repressor protein AbbA.
Article in Journal of molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 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
9 citing papers in PubMed.
- The alternative sigma factor SigN ofJournal of bacteriology · 2023Article
- Gene Regulation of Biofilm-Associated Functional Amyloids.Pathogens (Basel, Switzerland) · 2021Review
- Role of c-di-GMP in improving stress resistance of alginate-chitosan microencapsulated Bacillus subtilis cells in simulated digestive fluids.Biotechnology letters · 2021Article
- A Bacteriophage DNA Mimic Protein Employs a Non-specific Strategy to Inhibit the Bacterial RNA Polymerase.Frontiers in microbiology · 2021Article
- Interaction of ArmZ with the DNA-binding domain of MexZ induces expression ofAntimicrobial agents and chemotherapy · 2019Article
- AhpA is a peroxidase expressed during biofilm formation in Bacillus subtilis.MicrobiologyOpen · 2017Article
- Noncanonical DNA-binding mode of repressor and its disassembly by antirepressor.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Structure and DNA-binding traits of the transition state regulator AbrB.Structure (London, England : 1993) · 2014Article
- Biofilm formation by Bacillus subtilis: new insights into regulatory strategies and assembly mechanisms.Molecular microbiology · 2014Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors.
Funding
Abstract
Bacteria respond to adverse environmental conditions by switching on the expression of large numbers of genes that enable them to adapt to unfavorable circumstances. In Bacillus subtilis, many adaptive genes are under the negative control of the global transition state regulator, the repressor protein AbrB. Stressful conditions lead to the de-repression of genes under AbrB control. Contributing to this de-repression is AbbA, an anti-repressor that binds to and blocks AbrB from binding to DNA. Here, we have determined the NMR structure of the functional AbbA dimer, confirmed that it binds to the N-terminal DNA-binding domain of AbrB, and have provided an initial description for the interaction using computational docking procedures. Interestingly, we show that AbbA has structural and surface characteristics that closely mimic the DNA phosphate backbone, enabling it to readily carry out its physiological function.
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What OpenQuestion holds
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.