Characterization of the locus encoding the [Ni-Fe] sulfhydrogenase from the archaeon Pyrococcus furiosus: evidence for a relationship to bacterial sulfite reductases

Pedroni, Paola Maria; Volpe, Anna Della; Galli, G.; Mura, Giovanni Maria; Pratesi, Claudio; Grandi, Guido

doi:10.1099/13500872-141-2-449

Cited by 61 publications

(72 citation statements)

References 36 publications

(17 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Of these, 18 ORFs encode subunits associated with the three different hydrogenase systems that have been characterized from P. furiosus. These include those encoding six of the eight subunits of the two cytoplasmic hydrogenases (I and II [38,50]), whose expression decreases between 6-and 14-fold in the presence of S° (Table 1). Expression of the other two ORFs (encoding the ␣-and ␥-subunits of hydrogenase I) decrease by 2.2-to 4.8-fold.…”

Section: Resultsmentioning

confidence: 99%

DNA Microarray Analysis of the Hyperthermophilic Archaeon Pyrococcus furiosus : Evidence for a New Type of Sulfur-Reducing Enzyme Complex

2001

View full text Add to dashboard Cite

DNA microarrays were constructed by using 271 open reading frame (ORFs) from the genome of the archaeon Pyrococcus furiosus. They were used to investigate the effects of elemental sulfur (S°) on the levels of gene expression in cells grown at 95°C with maltose as the carbon source. The ORFs included those that are proposed to encode proteins mainly involved in the pathways of sugar and peptide catabolism, in the metabolism of metals, and in the biosynthesis of various cofactors, amino acids, and nucleotides. The expression of 21 ORFs decreased by more than fivefold when cells were grown with S°and, of these, 18 encode subunits associated with three different hydrogenase systems. The remaining three ORFs encode homologs of ornithine carbamoyltransferase and HypF, both of which appear to be involved in hydrogenase biosynthesis, as well as a conserved hypothetical protein. The expression of two previously uncharacterized ORFs increased by more than 25-fold when cells were grown with S°. Their products, termed SipA and SipB (for sulfur-induced proteins), are proposed to be part of a novel S°-reducing, membrane-associated, iron-sulfur cluster-containing complex. Two other previously uncharacterized ORFs encoding a putative flavoprotein and a second FeS protein were upregulated more than sixfold in S°-grown cells, and these are also thought be involved in S°r eduction. Four ORFs that encode homologs of proteins involved in amino acid metabolism were similarly upregulated in S°-grown cells, a finding consistent with the fact that growth on peptides is a S°-dependent process. An ORF encoding a homolog of the eukaryotic rRNA processing protein, fibrillarin, was also upregulated sixfold in the presence of S°, although the reason for this is as yet unknown. Of the 20 S°-independent ORFs that are the most highly expressed (at more than 20 times the detection limit), 12 of them represent enzymes purified from P. furiosus, but none of the products of the 34 S°-independent ORFs that are not expressed above the detection limit have been characterized. These results represent the first derived from the application of DNA microarrays to either an archaeon or a hyperthermophile.Hyperthermophiles are microorganisms that grow optimally at temperatures of 80°C and higher, and most are classified as archaea (65). They are a rather diverse group with respect to their metabolic capabilities, but many of them utilize peptides as a carbon source and reduce elemental sulfur (S°) to H 2 S (66). Of these, the majority are obligately proteolytic and show little if any growth unless S°is added to the growth medium. The exceptions include some species of Pyrococcus that metabolize poly-and oligosaccharides, as well as peptides (3, 4, 15). For example, Pyrococcus furiosus grows on a disaccharide (maltose) to high cell densities in the absence of S°and produces H 2 as an end product rather than H 2 S. On the other hand, P. furiosus requires S°in the growth medium when it utilizes peptides as a carbon source (1). A comparison of the activities of ...

show abstract

Section: Resultsmentioning

confidence: 99%

DNA Microarray Analysis of the Hyperthermophilic Archaeon Pyrococcus furiosus : Evidence for a New Type of Sulfur-Reducing Enzyme Complex

2001

View full text Add to dashboard Cite

show abstract

“…Electrons from H 2 would have been extracted by a membrane-associated hydrogenase and transferred across the membrane to two major pathways: (i) CO 2 reduction in methanogens and (ii) elementary sulfur reduction (38). The latter could have been mediated by a sulfur-reducing hydrogenase ancestor (41) or by an ancient sulfur-reducing domain (42). Interestingly, both of these functions are represented in the largest subnetwork (Fig.…”

Section: Does the Largest Subnetwork Contain Components Of Metabolicmentioning

confidence: 99%

Evolutionary history of redox metal-binding domains across the tree of life

Harel

Bromberg²,

Falkowski

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

Oxidoreductases mediate electron transfer (i.e., redox) reactions across the tree of life and ultimately facilitate the biologically driven fluxes of hydrogen, carbon, nitrogen, oxygen, and sulfur on Earth. The core enzymes responsible for these reactions are ancient, often small in size, and highly diverse in amino acid sequence, and many require specific transition metals in their active sites. Here we reconstruct the evolution of metal-binding domains in extant oxidoreductases using a flexible network approach and permissive profile alignments based on available microbial genome data. Our results suggest there were at least 10 independent origins of redox domain families. However, we also identified multiple ancient connections between Fe 2 S 2 -(adrenodoxin-like) and heme-(cytochrome c) binding domains. Our results suggest that these two iron-containing redox families had a single common ancestor that underwent duplication and divergence. The iron-containing protein family constitutes ∼50% of all metal-containing oxidoreductases and potentially catalyzed redox reactions in the Archean oceans. Heme-binding domains seem to be derived via modular evolutionary processes that ultimately form the backbone of redox reactions in both anaerobic and aerobic respiration and photosynthesis. The empirically discovered network allows us to peer into the ancient history of microbial metabolism on our planet.iron-sulfur | Great Oxidation/Oxygenation Event | biogeochemical cycles | core pathways

show abstract

“…In common with many other archaeal genes (Brown et al, 1989;Tiboni et al, 1993;Pedroni et Reeve et al, 1986), the dinucleotide CG is under-represented in coding regions.…”

Section: M O L I T O R a N D O T H E R Smentioning

confidence: 99%

A dissimilatory sirohaem-sulfite-reductase-type protein from the hyperthermophilic archaeon Pyrobaculum islandicum

et al. 1998

View full text Add to dashboard Cite

A sulf ite-reductase-type protein was purified from the hyperthermophilic crenarchaeote Pyrobaculum islandicum grown chemoorganoheterotrophically with thiosulfate as terminal electron acceptor. In common with dissimilatory sulfite reductases the protein has an a#* structure and contains high-spin sirohaem, non-haem iron and acid-labile sulfide. The oxidized protein exhibits absorption maxima a t 280,392, 578 and 710 nm with shoulders a t 430 and 610 nm. The isoelectric point of pH 8 4 sets the protein apart from all dissimilatory sulfite reductases characterized thus far. The genes for the a-and P-subunits (dsrA and dsrB) are contiguous in the order dsrAdsrB and most probably comprise an operon with the directly following dsrG and dsrC genes. dsrG and dsrC encode products which are homologous to eukaryotic glutathione S-transferases and the proposed y-subunit of Desulfovibrio vulgaris sulf ite reductase, respectively. dsrA and dsrB encode 44.2 kDa and 41.2 kDa peptides which show significant similarity to the two homologous subunits DsrA and DsrB of dissimilatory sulfite reductases. Phylogenetic analyses indicate a common protogenotic origin of the P. islandicum protein and the dissimilatory sulfite reductases from sulfate-reducing and sulfideoxidizing prokaryotes. However, the protein from P. islandicum and the sulfite reductases f rom sulfate-reducers and from sulf ur-oxidizers most probably evolved into three independent lineages prior to divergence of archaea and bacteria.

show abstract

Characterization of the locus encoding the [Ni-Fe] sulfhydrogenase from the archaeon Pyrococcus furiosus: evidence for a relationship to bacterial sulfite reductases

Cited by 61 publications

References 36 publications

DNA Microarray Analysis of the Hyperthermophilic Archaeon Pyrococcus furiosus : Evidence for a New Type of Sulfur-Reducing Enzyme Complex

DNA Microarray Analysis of the Hyperthermophilic Archaeon Pyrococcus furiosus : Evidence for a New Type of Sulfur-Reducing Enzyme Complex

Evolutionary history of redox metal-binding domains across the tree of life

A dissimilatory sirohaem-sulfite-reductase-type protein from the hyperthermophilic archaeon Pyrobaculum islandicum

Contact Info

Product

Resources

About