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PMID: 15687204 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

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.

Journal of bacteriology ·Vol. 187 ·No. 4 ·2005-02-00 ·Pages 1392-404

Dahl C, Engels S, Pott-Sperling AS, Schulte A, Sander J, Lübbe Y, Deuster O, Brune DC

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.

MeSH Terms
Bacterial Proteins/genetics,isolation & purification,metabolism Blotting, Western Chromatiaceae/genetics,metabolism Cytochromes c/genetics,metabolism DNA, Bacterial/chemistry Genes, Bacterial Iron-Sulfur Proteins/genetics,metabolism Membrane Proteins/genetics,metabolism Molecular Sequence Data Molecular Weight Multigene Family NADH, NADPH Oxidoreductases/genetics,metabolism Operon Oxidation-Reduction Oxidoreductases Acting on Sulfur Group Donors/isolation & purification Protein Interaction Mapping Protein Subunits/isolation & purification Sequence Analysis, DNA Sulfides/metabolism Sulfur/metabolism Thiosulfates/metabolism Transaminases/genetics,metabolism
Chemicals
Bacterial Proteins DNA, Bacterial Iron-Sulfur Proteins Membrane Proteins Protein Subunits Sulfides Thiosulfates Sulfur Cytochromes c NADH, NADPH Oxidoreductases Oxidoreductases Acting on Sulfur Group Donors Transaminases cobyrinic acid a,c-diamide synthase
Authors & Affiliations
8 authors, click to expand affiliations / ORCID
Dahl Christiane
Institut für Mikrobiologie & Biotechnologie, Rheinische Friedrich-Wilhelms-Universität Bonn, Meckenheimer Allee 168, D-53115 Bonn, Germany. ChDahl@uni-bonn.de
Engels Sabine
Pott-Sperling Andrea S
Schulte Andrea
Sander Johannes
Lübbe Yvonne
Deuster Oliver
Brune Daniel C
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
DOI
10.1128/JB.187.4.1392-1404.2005
Email
chdahl@uni-bonn.de
Published
2005-02-00
Pages
1392-404
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC545617
Subset
IM
Databases
GENBANK
U84760
External Links
PubMed source DOI: 10.1128/JB.187.4.1392-1404.2005 PMC Full Text View journal details
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