ArticleThe Journal of biological chemistry2014
New proteins involved in sulfur trafficking in the cytoplasm of Allochromatium vinosum.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 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
31 citing papers in PubMed, 48 citations in OpenAlex.
- Insights into the Versatile Sulfur Metabolism ofMicroorganisms · 2026Article
- The genetic repertoire underlying electrogenic sulphur oxidation in cable bacteria.BMC genomics · 2026Article
- Sulfur disproportionation occurs globally across anoxic habitats and has multiple mechanisms of independent evolutionary origin.The ISME journal · 2026Review
- Distribution of a novel DsrEFH sulfur transferase suggests widespread sulfur oxidation capacity in sulfate reducers.The ISME journal · 2026Article
- Dual Roles of Reducing Systems in Protein Persulfidation and Depersulfidation.Antioxidants (Basel, Switzerland) · 2025Review
- Growth physiology, genomics, and proteomics ofFrontiers in microbiology · 2025Article
- Mechanism of Intracellular Elemental Sulfur Oxidation inInternational journal of molecular sciences · 2024Article
- Evidence for autotrophic growth of purple sulfur bacteria using pyrite as electron and sulfur source.Applied and environmental microbiology · 2024Article
- A cascade of sulfur transferases delivers sulfur to the sulfur-oxidizing heterodisulfide reductase-like complex.Protein science : a publication of the Protein Society · 2024Article
- YeeD is an essential partner for YeeE-mediated thiosulfate uptake in bacteria and regulates thiosulfate ion decomposition.PLoS biology · 2024Article
- The Complete Genome of a Novel Typical SpeciesMicroorganisms · 2024Article
- Metabolic and phylogenetic diversity in the phylumISME communications · 2024Article
- Ecophysiology and interactions of a taurine-respiring bacterium in the mouse gut.Nature communications · 2023Article
- A sulfide-sensor and a sulfane sulfur-sensor collectively regulate sulfur-oxidation for feather degradation by Bacillus licheniformis.Communications biology · 2023Article
- Article
- Allochromatium tepidum, sp. nov., a hot spring species of purple sulfur bacteria.Archives of microbiology · 2022Article
- Physiological and comparative proteomic characterization ofFrontiers in microbiology · 2022Article
- DiSCo: a sequence-based type-specific predictor of Dsr-dependent dissimilatory sulphur metabolism in microbial data.Microbial genomics · 2021Article
- TusA Is a Versatile Protein That Links Translation Efficiency to Cell Division in Escherichia coli.Journal of bacteriology · 2021Article
- 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
No grant is acknowledged in the PubMed record.
Abstract
The formation of periplasmic sulfur globules is an intermediate step during the oxidation of reduced sulfur compounds in various sulfur-oxidizing microorganisms. The mechanism of how this sulfur is activated and crosses the cytoplasmic membrane for further oxidation to sulfite by the dissimilatory reductase DsrAB is incompletely understood, but it has been well documented that the pathway involves sulfur trafficking mediated by sulfur-carrying proteins. So far sulfur transfer from DsrEFH to DsrC has been established. Persulfurated DsrC very probably serves as a direct substrate for DsrAB. Here, we introduce further important players in oxidative sulfur metabolism; the proteins Rhd_2599, TusA, and DsrE2 are strictly conserved in the Chromatiaceae, Chlorobiaceae, and Acidithiobacillaceae families of sulfur-oxidizing bacteria and are linked to genes encoding complexes involved in sulfur oxidation (Dsr or Hdr) in the latter two. Here we show via relative quantitative real-time PCR and microarray analysis an increase of mRNA levels under sulfur-oxidizing conditions for rhd_2599, tusA, and dsrE2 in Allochromatium vinosum. Transcriptomic patterns for the three genes match those of major genes for the sulfur-oxidizing machinery rather than those involved in biosynthesis of sulfur-containing biomolecules. TusA appears to be one of the major proteins in A. vinosum. A rhd_2599-tusA-dsrE2-deficient mutant strain, although not viable in liquid culture, was clearly sulfur oxidation negative upon growth on solid media containing sulfide. Rhd_2599, TusA, and DsrE2 bind sulfur atoms via conserved cysteine residues, and experimental evidence is provided for the transfer of sulfur between these proteins as well as to DsrEFH and DsrC.
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.