Specificity of respiratory pathways involved in the reduction of sulfur compounds by Salmonella enterica

Hinsley, Andrew P.; Berks, Ben C.

doi:10.1099/00221287-148-11-3631

Cited by 83 publications

(84 citation statements)

References 24 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…However, homologs of the E. coli REMPs are found in many bacteria (129). Expression of the apparently REMP-less Tat substrate PhsABC from S. enterica LT2 in E. coli led to the production of active thiosulfate reductase (59). This finding suggests that either a REMP is not required for the export of PhsABC or that E. coli REMPs compensate for the lack of the native chaperone.…”

Section: Folding Quality Controlmentioning

confidence: 54%

The Bacterial Twin-Arginine Translocation Pathway

Lee

Tullman‐Ercek

Georgiou

2006

Annu. Rev. Microbiol.

296

241

View full text Add to dashboard Cite

The twin-arginine translocation (Tat) pathway is responsible for the export of folded proteins across the cytoplasmic membrane of bacteria. Substrates for the Tat pathway include redox enzymes requiring cofactor insertion in the cytoplasm, multimeric proteins that have to assemble into a complex prior to export, certain membrane proteins, and proteins whose folding is incompatible with Sec export. These proteins are involved in a diverse range of cellular activities including anaerobic metabolism, cell envelope biogenesis, metal acquisition and detoxification, and virulence. The Escherichia coli translocase consists of the TatA, TatB, and TatC proteins, but little is known about the precise sequence of events that leads to protein translocation, the energetic requirements, or the mechanism that prevents the export of misfolded proteins. Owing to the unique characteristics of the pathway, it holds promise for biotechnological applications.

show abstract

Section: Folding Quality Controlmentioning

confidence: 54%

The Bacterial Twin-Arginine Translocation Pathway

Lee

Tullman‐Ercek

Georgiou

2006

Annu. Rev. Microbiol.

296

241

View full text Add to dashboard Cite

show abstract

“…One of these groups is made up of thiosulfate, tetrathionate, polysulfide, and sulfur reductases. Sequence comparison between the members of this group showed that a cysteine residue is conserved and could coordinate the molybdenum atom (41,47). This conserved cysteine is also found in SreA from A. aeolicus (Cys-176) (Fig.…”

Section: Purification Of a Membrane-bound Sulfur-reducingmentioning

confidence: 81%

“…The SR enzymes form a specific group distinct from other molybdopterin-guanine dinucleotide-dependent enzymes in the Me 2 SO reductase family (41).…”

Section: Purification Of a Membrane-bound Sulfur-reducingmentioning

confidence: 99%

A Membrane-bound Multienzyme, Hydrogen-oxidizing, and Sulfur-reducing Complex from the Hyperthermophilic Bacterium Aquifex aeolicus

Guiral

Tron

Aubert

et al. 2005

Journal of Biological Chemistry

104

View full text Add to dashboard Cite

Aquifex aeolicus is a hyperthermophilic, chemolithoautotrophic, hydrogen-oxidizing, and microaerophilic bacterium growing at 85°C. We have shown that it can grow on an H 2 /S°medium and produce H 2 S from sulfur in the later exponential phase. The complex carrying the sulfur reducing activity (electron transport from H 2 to S°) has been purified and characterized. It is a membranebound multiprotein complex containing a [NiFe] hydrogenase and a sulfur reductase connected via quinones. The sulfur reductase is encoded by an operon annotated dms (dimethyl sulfoxide reductase) that we have renamed sre and is composed of three subunits. Sequence analysis showed that it belongs to the Me 2 SO reductase molybdoenzyme family and is similar to the sulfur/polysulfide/thiosulfate/tetrathionate reductases. The study of catalytic properties clearly demonstrated that it can reduce tetrathionate, sulfur, and polysulfide, but cannot reduce Me 2 SO and thiosulfate, and that NADPH increases the sulfur reducing activity. To date, this is the first characterization of a supercomplex from a bacterium that couples hydrogen oxidation and sulfur reduction. The distinctive feature in A. aeolicus is the cytoplasmic localization of the sulfur reduction, which is in accordance with the presence of sulfur globules in the cytoplasm. Association of this sulfur-reducing complex with a hydrogen-oxygen pathway complex (hydrogenase I, bc 1 complex) in the membrane suggests that subcomplexes involved in respiratory chains in this bacterium are part of supramolecular organization.The production of biomass in extreme light-independent environments is energized by chemolithoautotrophic oxidation and reduction of inorganic compounds like elemental sulfur (S°), 2 hydrogen, and nitrate (1, 2). Sulfur and sulfur compounds are the most abundant sources of both electron acceptors and electron donors in extremophilic environments (like volcanic environments) and are used by many microorganisms to support growth (3-6). Reduction and oxidation of sulfur compounds (sulfate, sulfite, thiosulfate, organic sulfoxide, elemental sulfur, polysulfides, and organic disulfide) are vital processes for many bacteria and essential steps in the global sulfur cycle. Because of the multiple oxidation states of sulfur, the biochemistry and chemistry of this cycle are complex and still not completely understood (7,8). This problem is exacerbated by the reactivities of the sulfur species at various oxidation states toward each other (7). The ability to reduce elemental sulfur is mostly found among hyperthermophilic micro-organisms (Archaea and Bacteria) (8), the majority of which depend on S°reduc-tion for optimal growth. They use either molecular hydrogen or organic compounds as electron donors. It has been suggested that S°respiration is one of the earliest mechanisms for energy conservation, because the hyperthermophiles are the forms of life evolving the most slowly (9).The processes by which micro-organisms reduce S°to H 2 S are still unclear for most of them, and only few ...

show abstract

“…For both SMTZ-45 and SMTZ1-45 the closest NCBI hits to the thiosulfate reductase included a 4Fe-4S ferredoxin isolated from Desulfobacterium autotrophicum (Brysch et al, 1987), an Enterobacteriacea thiosulfate reductase electron transporter (phsB) (Brenner, 1983) and the polysulfide reductase subunit B of Citrobacter freundii (Sakazaki, 1984). The phs operon codes for a molybdopterin cofactor that uses cysteine residues to bind and break the di-sulfur bonds (Hinsley and Berks, 2002). Homologs for these cysteine residues and for the iron sulfur clusters responsible for electron transfer have been identified on the phsB gene (Heinzinger et al, 1995).…”

Section: The Possible Role Of Thorarchaeota In Sulfur Cyclingmentioning

confidence: 99%

Genomic reconstruction of a novel, deeply branched sediment archaeal phylum with pathways for acetogenesis and sulfur reduction

Seitz¹,

et al. 2016

View full text Add to dashboard Cite

Marine and estuary sediments contain a variety of uncultured archaea whose metabolic and ecological roles are unknown. De novo assembly and binning of high-throughput metagenomic sequences from the sulfate-methane transition zone in estuary sediments resulted in the reconstruction of three partial to near-complete (2.4-3.9 Mb) genomes belonging to a previously unrecognized archaeal group. Phylogenetic analyses of ribosomal RNA genes and ribosomal proteins revealed that this group is distinct from any previously characterized archaea. For this group, found in the White Oak River estuary, and previously registered in sedimentary samples, we propose the name 'Thorarchaeota'. The Thorarchaeota appear to be capable of acetate production from the degradation of proteins. Interestingly, they also have elemental sulfur and thiosulfate reduction genes suggesting they have an important role in intermediate sulfur cycling. The reconstruction of these genomes from a deeply branched, widespread group expands our understanding of sediment biogeochemistry and the evolutionary history of Archaea.

show abstract

Specificity of respiratory pathways involved in the reduction of sulfur compounds by Salmonella enterica

Cited by 83 publications

References 24 publications

The Bacterial Twin-Arginine Translocation Pathway

The Bacterial Twin-Arginine Translocation Pathway

A Membrane-bound Multienzyme, Hydrogen-oxidizing, and Sulfur-reducing Complex from the Hyperthermophilic Bacterium Aquifex aeolicus

Genomic reconstruction of a novel, deeply branched sediment archaeal phylum with pathways for acetogenesis and sulfur reduction

Contact Info

Product

Resources

About