ArticleThe Journal of biological chemistry2012
The Bacillus subtilis chemoreceptor McpC senses multiple ligands using two discrete mechanisms.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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.
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.
Who cites it
41 citing papers in PubMed, 81 citations in OpenAlex.
- Amino Acids From Root Exudates Induce Bacillus Spore Germination to Enhance Root Colonisation and Plant Growth Promotion.Microbial biotechnology · 2025Article
- Bacterial amino acid chemotaxis: a widespread strategy with multiple physiological and ecological roles.Journal of bacteriology · 2024Review
- Negative chemotaxis of Ligilactobacillus agilis BKN88 against gut-derived substances.Scientific reports · 2023Article
- Sensing preferences for prokaryotic solute binding protein families.Microbial biotechnology · 2023Article
- Three unrelated chemoreceptors provide Pectobacterium atrosepticum with a broad-spectrum amino acid sensing capability.Microbial biotechnology · 2023Article
- Is it possible to predict signal molecules that are recognized by bacterial receptors?Environmental microbiology · 2023Article
- Zinc solubilizing bacteria and their potential as bioinoculant for growth promotion of green soybean (PeerJ · 2023Article
- Diverse Sensory Repertoire of Paralogous Chemoreceptors Tlp2, Tlp3, and Tlp4 inMicrobiology spectrum · 2022Article
- The Repertoire of Solute-Binding Proteins of Model Bacteria Reveals Large Differences in Number, Type, and Ligand Range.Microbiology spectrum · 2022Article
- Signal binding at both modules of its dCache domain enables the McpA chemoreceptor ofProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Noncanonical Sensing Mechanisms for Bacillus subtilis Chemoreceptors.Journal of bacteriology · 2022Article
- Characterization of Opposing Responses to Phenol by Bacillus subtilis Chemoreceptors.Journal of bacteriology · 2022Article
- Chemotaxis of Beneficial Rhizobacteria to Root Exudates: The First Step towards Root-Microbe Rhizosphere Interactions.International journal of molecular sciences · 2021Review
- The role of solute binding proteins in signal transduction.Computational and structural biotechnology journal · 2021Review
- The Unconventional Cytoplasmic Sensing Mechanism for Ethanol Chemotaxis in Bacillus subtilis.mBio · 2020Article
- Structure-Activity Relationship Study Reveals the Molecular Basis for Specific Sensing of Hydrophobic Amino Acids by theBiomolecules · 2020Article
- The Mechanism of Bidirectional pH Taxis in Bacillus subtilis.Journal of bacteriology · 2020Article
- Article
- Determination of Ligand Profiles forInternational journal of molecular sciences · 2019Article
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Bacillus subtilis can perform chemotaxis toward all 20 L-amino acids normally found in proteins. Loss of a single chemoreceptor, McpC, was previously found to reduce chemotaxis to 19 of these amino acids. In this study, we investigated the amino acid-sensing mechanism of McpC. We show that McpC alone can support chemotaxis to 17 of these amino acids to varying degrees. Eleven amino acids were found to directly bind the amino-terminal sensing domain of McpC in vitro. Sequence analysis indicates that the McpC sensing domain exhibits a dual Per-Arnt-Sim (PAS) domain structure. Using this structure as a guide, we were able to isolate mutants that suggest that four amino acids (arginine, glutamine, lysine, and methionine) are sensed by an indirect mechanism. We identified four candidate binding lipoproteins associated with amino acid transporters that may function in indirect sensing: ArtP, GlnH, MetQ, and YckB. ArtP was found to bind arginine and lysine; GlnH, glutamine; MetQ, methionine; and YckB, tryptophan. In addition, we found that ArtP, MetQ, and YckB bind the sensing domain of McpC, suggesting that the three participate in the indirect sensing of arginine, lysine, methionine, and possibly tryptophan as well. Taken together, these results further our understanding of amino acid chemotaxis in B. subtilis and gain insight into how a single chemoreceptor is able to sense many amino acids.
Indexed as
Identifiers
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.