Evidence map›Paper›PMID 31493408›Full record

ArticleJournal of molecular biology2020

The Solution Structures and Interaction of SinR and SinI: Elucidating the Mechanism of Action of the Master Regulator Switch for Biofilm Formation in Bacillus subtilis.

Morgan E Milton, G Logan Draughn, Benjamin G Bobay, Sean D Stowe, Andrew L Olson, Erik A Feldmann, Richele J Thompson, Katherine H Myers, Michael T Santoro, Daniel B Kearns and 1 more

Abstract read
In one paragraph

Article in Journal of molecular biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

20 citing papers in PubMed.

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  18. Spo0A SuppressesmSphere · 2020
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

11 authors.

Morgan E MiltonDepartment of Biochemistry and Molecular Biology, The Brody School of Medicine, East Carolina University, Greenville, NC 27834, USA.
G Logan DraughnDepartment of Molecular and Structural Biochemistry, North Carolina State University, Raleigh, NC 27695, USA.
Benjamin G BobayDepartment of Molecular and Structural Biochemistry, North Carolina State University, Raleigh, NC 27695, USA; Duke University NMR Center, Duke University, Durham, NC 27710, USA.
Sean D StoweDepartment of Molecular and Structural Biochemistry, North Carolina State University, Raleigh, NC 27695, USA.
Andrew L OlsonDepartment of Molecular and Structural Biochemistry, North Carolina State University, Raleigh, NC 27695, USA.
Erik A FeldmannDepartment of Molecular and Structural Biochemistry, North Carolina State University, Raleigh, NC 27695, USA.
Richele J ThompsonDepartment of Biochemistry and Molecular Biology, The Brody School of Medicine, East Carolina University, Greenville, NC 27834, USA.
Katherine H MyersDepartment of Molecular and Structural Biochemistry, North Carolina State University, Raleigh, NC 27695, USA.
Michael T SantoroDepartment of Molecular and Structural Biochemistry, North Carolina State University, Raleigh, NC 27695, USA.
Daniel B KearnsDepartment of Biology, Indiana University Bloomington, Bloomington, IN 47405, USA.
John CavanaghDepartment of Biochemistry and Molecular Biology, The Brody School of Medicine, East Carolina University, Greenville, NC 27834, USA. Electronic address: cavanaghj19@ecu.edu.

Funding

NMR STUDIES OF BACTERIAL REGULATORY PROTEINSR01GM055769 · NIGMS · WADSWORTH CENTER · PI CAVANAGH, JOHN, MELANDER, CHRISTIAN COREY · 1998 to 2017
$3.8M
NIGMS NIH HHS R01 GM055769
6 · The paper itself

Abstract

Bacteria have developed numerous protection strategies to ensure survival in harsh environments, with perhaps the most robust method being the formation of a protective biofilm. In biofilms, bacterial cells are embedded within a matrix that is composed of a complex mixture of polysaccharides, proteins, and DNA. The gram-positive bacterium Bacillus subtilis has become a model organism for studying regulatory networks directing biofilm formation. The phenotypic transition from a planktonic to biofilm state is regulated by the activity of the transcriptional repressor, SinR, and its inactivation by its primary antagonist, SinI. In this work, we present the first full-length structural model of tetrameric SinR using a hybrid approach combining high-resolution solution nuclear magnetic resonance (NMR), chemical cross-linking, mass spectrometry, and molecular docking. We also present the solution NMR structure of the antagonist SinI dimer and probe the mechanism behind the SinR-SinI interaction using a combination of biochemical and biophysical techniques. As a result of these findings, we propose that SinI utilizes a residue replacement mechanism to block SinR multimerization, resulting in diminished DNA binding and concomitant decreased repressor activity. Finally, we provide an evidence-based mechanism that confirms how disruption of the SinR tetramer by SinI regulates gene expression.

Indexed as

Amino Acid SequenceBacillus subtilisBacterial ProteinsBiofilmsDNA-Binding ProteinsGene Expression Regulation, BacterialMolecular Docking SimulationMutationProtein BindingProtein ConformationBacterial ProteinsDNA-Binding ProteinsFlaD protein, BacteriaSinI protein, Bacillus subtilisBacillus subtilisBiofilmsNMR solution structureTranscriptional regulation

Identifiers

PMID31493408
PMCPMC7384550

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Registered trials

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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.