ArticleJournal of bacteriology2012
Signal perception by the secretion stress-responsive CssRS two-component system in Bacillus subtilis.
Article in Journal of bacteriology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 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
16 citing papers in PubMed, 27 citations in OpenAlex.
- Multi-parameter optimization of recombinant protein secretion in Bacillus subtilis: a review.Microbial cell factories · 2026Review
- The gram-positive HtrA, the protease that is also a chaperone.Journal of bacteriology · 2026Review
- The conserved two-component systems CutRS and CssRS control the protein secretion stress response inmBio · 2026Article
- Protein trafficking across the cell envelope of gram-positive bacteria.Journal of bacteriology · 2025Review
- The CssRS two-component system of Bacillus subtilis contributes to teicoplanin and polymyxin B response.Folia microbiologica · 2025Article
- Bacterial Growth Temperature as a Horizontally Acquired Polygenic Trait.Genome biology and evolution · 2025Article
- HtrAs are essential for the survival of the haloarchaeonApplied and environmental microbiology · 2024Article
- Giving a signal: how protein phosphorylation helps Bacillus navigate through different life stages.FEMS microbiology reviews · 2023Review
- Emerging Roles of Functional Bacterial Amyloids in Gene Regulation, Toxicity, and Immunomodulation.Microbiology and molecular biology reviews : MMBR · 2020Review
- Identification and optimization of PrsA in Bacillus subtilis for improved yield of amylase.Microbial cell factories · 2019Article
- Microdomain formation is a general property of bacterial membrane proteins and induces heterogeneity of diffusion patterns.BMC biology · 2018Article
- Stabilization of Bacillus subtilis Spx under cell wall stress requires the anti-adaptor protein YirB.PLoS genetics · 2018Article
- Release of an HtrA-Like Protease from the Cell Surface of ThermophilicFrontiers in microbiology · 2017Article
- Regulation of bacterial heat shock stimulons.Cell stress & chaperones · 2016Review
- Degradation of extracytoplasmic catalysts for protein folding in Bacillus subtilis.Applied and environmental microbiology · 2014Article
- Fermentation stage-dependent adaptations of Bacillus licheniformis during enzyme production.Microbial cell factories · 2013Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The CssRS two-component system responds to heat and secretion stresses in Bacillus subtilis by controlling expression of HtrA and HtrB chaperone-type proteases and positively autoregulating its own expression. Here we report on the features of the CssS extracellular loop domain that are involved in signal perception and on CssS subcellular localization. Individual regions of the CssS extracellular loop domain contribute differently to signal perception and activation. The conserved hydrophilic 26-amino-acid segment juxtaposed to transmembrane helix 1 is involved in the switch between the deactivated and activated states, while the conserved 19-amino-acid hydrophobic segment juxtaposed to transmembrane 2 is required for signal perception and/or transduction. Perturbing the size of the extracellular loop domain increases CssS kinase activity and makes it unresponsive to secretion stress. CssS is localized primarily at the septum but is also found in a punctate pattern with lower intensity throughout the cell cylinder. Moreover, the CssRS-controlled HtrA and HtrB proteases are randomly distributed in foci throughout the cell surface, with more HtrB than HtrA foci in unstressed cells.
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.