ArticleJournal of bacteriology2005
Novel genes of the dsr gene cluster and evidence for close interaction of Dsr proteins during sulfur oxidation in the phototrophic sulfur bacterium Allochromatium vinosum.
Article in Journal of bacteriology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 90 papers.
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90 citing papers in PubMed, 224 citations in OpenAlex.
- A Two-Step SeCys Oxidation Pathway Bridging Soil Selenium Bioavailability and Rice Selenium Biofortification.Environmental microbiology · 2026Article
- TusDCB-mediated tRNA sulfur modification is required for virulence and intestinal fitness in enterohemorrhagicInfection and immunity · 2026Article
- Genomic and functional characterization of Pseudosulfitobacter pseudonitzschiae BPC-C4-2: a growth-promoting symbiont in Antarctic Ulva communities.BMC genomics · 2026Article
- Distribution of a novel DsrEFH sulfur transferase suggests widespread sulfur oxidation capacity in sulfate reducers.The ISME journal · 2026Article
- Genetic isolation and metabolic complexity of an Antarctic subglacial microbiome.Nature communications · 2025Article
- Adaptive modifications in plant sulfur metabolism over evolutionary time.Journal of experimental botany · 2024Review
- Microbial assemblages and associated biogeochemical processes in Lake Bonney, a permanently ice-covered lake in the McMurdo Dry Valleys, Antarctica.Environmental microbiome · 2024Article
- Evidence for autotrophic growth of purple sulfur bacteria using pyrite as electron and sulfur source.Applied and environmental microbiology · 2024Article
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- TusDCB, a sulfur transferase complex involved in tRNA modification, contributes to UPEC pathogenicity.Scientific reports · 2024Article
- Evolutionary history and origins of Dsr-mediated sulfur oxidation.The ISME journal · 2024Article
- Microbial communities related to the sulfur cycle in the Sansha Yongle Blue Hole.Microbiology spectrum · 2023Article
- Stepwise pathway for early evolutionary assembly of dissimilatory sulfite and sulfate reduction.The ISME journal · 2023Article
- Fluorescence Microscopy Study of the Intracellular Sulfur Globule Protein SgpD in the Purple Sulfur BacteriumMicroorganisms · 2023Article
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- Sulfur-oxidizing bacteria (SOB) and sulfate-reducing bacteria (SRB) in oil reservoir and biological control of SRB: a review.Archives of microbiology · 2023Review
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- Novel antimicrobial activity of protein produced by Streptomyces lividans TK24 against the phytopathogen Clavibacter michiganensis.Archives of microbiology · 2022Article
- Metagenomic insights into the functions of microbial communities in sulfur-rich sediment of a shallow-water hydrothermal vent off Kueishan Island.Frontiers in microbiology · 2022Article
- Heterotrophic Sulfur Oxidation ofFrontiers in microbiology · 2022Article
30 more citing papers are in PubMed but not listed here.
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8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Seven new genes designated dsrLJOPNSR were identified immediately downstream of dsrABEFHCMK, completing the dsr gene cluster of the phototrophic sulfur bacterium Allochromatium vinosum D (DSM 180(T)). Interposon mutagenesis proved an essential role of the encoded proteins for the oxidation of intracellular sulfur, an obligate intermediate during the oxidation of sulfide and thiosulfate. While dsrR and dsrS encode cytoplasmic proteins of unknown function, the other genes encode a predicted NADPH:acceptor oxidoreductase (DsrL), a triheme c-type cytochrome (DsrJ), a periplasmic iron-sulfur protein (DsrO), and an integral membrane protein (DsrP). DsrN resembles cobyrinic acid a,c-diamide synthases and is probably involved in the biosynthesis of siro(heme)amide, the prosthetic group of the dsrAB-encoded sulfite reductase. The presence of most predicted Dsr proteins in A. vinosum was verified by Western blot analysis. With the exception of the constitutively present DsrC, the formation of Dsr gene products was greatly enhanced by sulfide. DsrEFH were purified from the soluble fraction and constitute a soluble alpha(2)beta(2)gamma(2)-structured 75-kDa holoprotein. DsrKJO were purified from membranes pointing at the presence of a transmembrane electron-transporting complex consisting of DsrKMJOP. In accordance with the suggestion that related complexes from dissimilatory sulfate reducers transfer electrons to sulfite reductase, the A. vinosum Dsr complex is copurified with sulfite reductase, DsrEFH, and DsrC. We therefore now have an ideal and unique possibility to study the interaction of sulfite reductase with other proteins and to clarify the long-standing problem of electron transport from and to sulfite reductase, not only in phototrophic bacteria but also in sulfate-reducing prokaryotes.
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