Complete Genome Sequence of “Vulcanisaeta moutnovskia” Strain 768-28, a Novel Member of the Hyperthermophilic Crenarchaeal Genus Vulcanisaeta

Gumerov, Vadim M.; Mardanov, Andrey V.; Beletsky, Alexey V.; Prokofeva, M. I.; Bonch-Osmolovskaya, E. A.; Ravin, Nikolai V.; Skryabin, K. G.

doi:10.1128/jb.00237-11

Cited by 37 publications

(20 citation statements)

References 9 publications

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“…TVN0292 possessed a putative DNA binding helix, metal binding site 1, metal binding site 2, structural Zn 2+ binding site, and dimer interface regions (data not shown), all suggesting that TVN0292 is a Fur-like protein. TvFur was closely related to the Fur of Thermoplasma acidophilum (Ruepp et al, 2000) with Expect value 1e 89 and 86% identities, and more distantly related to the Fur of thermoacidophilic archaea or bacteria [ 35% identity with Fur of Alicyclobacillus acidocaldarius (Mavromatis et al, 2010), Metallosphaera cuprina (Liu et al, 2011) and Vulcanisaeta moutnovskia (Gumerov et al, 2011) ]. The homologous regions among these proteins were converged not only on the DNA binding domain but extended to the overall amino acid (data not shown).…”

Section: Expression and Purifi Cation Of Tvfurmentioning

confidence: 99%

Transcriptional factor Fur from Thermoplasma volcanium binds its own promoter DNA in a divalent cation-dependent manner

Ikeda

Minoshima

Satoh

et al. 2012

J. Gen. Appl. Microbiol.

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Because archaea possess many respiratory enzymes or radical scavengers with catalytic domains that contain iron, the expression of the genes encoding these enzymes might be regulated by iron acquisition. The genome of an archaeon, Thermoplasma volcanium contains a gene that encodes Fur (TVN0292). The fur gene of T. volcanium was amplifi ed by PCR, and cloned into plasmid pET28a. TvFur (T. volcanium Fur protein) was expressed in E. coli cells and then purifi ed. EMSA revealed that TvFur binds to its own promoter DNA. The binding to its own promoter was in an Mn 2+ -, Zn

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Section: Expression and Purifi Cation Of Tvfurmentioning

confidence: 99%

Transcriptional factor Fur from Thermoplasma volcanium binds its own promoter DNA in a divalent cation-dependent manner

Ikeda

Minoshima

Satoh

et al. 2012

J. Gen. Appl. Microbiol.

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“…The “aerobic-type” RBR phylogenetic tree (using an appropriate outgroup) showed that the closest clade to the root of the group comprises a set of orthologs from archaeal members ( Figure 2B in summary and Supplementary Figure S2 in detail) from the Vulcanisaeta, Caldivirga , and Thermoproteus genera of the Thermoproteales order (Itoh et al, 1999; Mavromatis et al, 2010; Gumerov et al, 2011; Mardanov et al, 2011). All of the extant members of this group are hyperthermophiles and are slightly acidophilic (pH 3.0–6.5).…”

Section: Resultsmentioning

confidence: 99%

Aerobic Lineage of the Oxidative Stress Response Protein Rubrerythrin Emerged in an Ancient Microaerobic, (Hyper)Thermophilic Environment

2016

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Rubrerythrins (RBRs) are non-heme di-iron proteins belonging to the ferritin-like superfamily. They are involved in oxidative stress defense as peroxide scavengers in a wide range of organisms. The vast majority of RBRs, including classical forms of this protein, contain a C-terminal rubredoxin-like domain involved in electron transport that is used during catalysis in anaerobic conditions. Rubredoxin is an ancient and large protein family of short length (<100 residues) that contains a Fe-S center involved in electron transfer. However, functional forms of the enzyme lacking the rubredoxin-like domain have been reported (e.g., sulerythrin and ferriperoxin). In this study, phylogenomic evidence is presented that suggests that a complete lineage of rubrerythrins, lacking the rubredoxin-like domain, arose in an ancient microaerobic and (hyper)thermophilic environments in the ancestors of the Archaea Thermoproteales and Sulfolobales. This lineage (termed the “aerobic-type” lineage) subsequently evolved to become adapted to environments with progressively lower temperatures and higher oxygen concentrations via the acquisition of two co-localized genes, termed DUF3501 and RFO, encoding a conserved protein of unknown function and a predicted Fe-S oxidoreductase, respectively. Proposed Horizontal Gene Transfer events from these archaeal ancestors to Bacteria expanded the opportunities for further evolution of this RBR including adaption to lower temperatures. The second lineage (termed the cyanobacterial lineage) is proposed to have evolved in cyanobacterial ancestors, maybe in direct response to the production of oxygen via oxygenic photosynthesis during the Great Oxygen Event (GOE). It is hypothesized that both lineages of RBR emerged in a largely anaerobic world with “whiffs” of oxygen and that their subsequent independent evolutionary trajectories allowed microorganisms to transition from this anaerobic world to an aerobic one.

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“…This organism was isolated from solfataric fields close to the Moutnovsky volcano in Kamchatka, Russia. Its growth temperature ranges between 333 and 371 K (Gumerov et al, 2011). VmoLac shares $50% sequence identity with other PLLs.…”

Section: Introductionmentioning

confidence: 99%

“…VmoLac (YP_004245953) is an enzyme identified from the recently sequenced crenarchaeon Vulcanisaeta moutnovskia strain 768-28 (Gumerov et al, 2011). This organism was isolated from solfataric fields close to the Moutnovsky volcano in Kamchatka, Russia.…”

Section: Introductionmentioning

confidence: 99%

Crystallization and preliminary X-ray diffraction analysis of the lactonaseVmoLac fromVulcanisaeta moutnovskia

et al. 2013

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Phosphotriesterase-like lactonases (PLLs) are native lactonases that are capable of hydrolyzing lactones such as aliphatic lactones or acyl-homoserine lactones, which are involved in bacterial quorum sensing. Previously characterized PLLs are moreover endowed with a promiscuous phosphotriesterase activity and are therefore able to detoxify organophosphate insecticides. A novel PLL representative, dubbed VmoLac, has been identified from the hyperthermophilic crenarchaeon Vulcanisaeta moutnovskia. Because of its intrinsic high thermal stability, VmoLac may constitute an appealing candidate for engineering studies with the aim of producing an efficient biodecontaminant for organophosphorus compounds and a bacterial antivirulence agent. In combination with biochemical studies, structural information will allow the identification of the residues involved in substrate specificity and an understanding of the enzymatic catalytic mechanisms. Here, the expression, purification, crystallization and X-ray data collection at 2.4 Å resolution of VmoLac are reported.

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Complete Genome Sequence of “Vulcanisaeta moutnovskia” Strain 768-28, a Novel Member of the Hyperthermophilic Crenarchaeal Genus Vulcanisaeta

Cited by 37 publications

References 9 publications

Transcriptional factor Fur from Thermoplasma volcanium binds its own promoter DNA in a divalent cation-dependent manner

Transcriptional factor Fur from Thermoplasma volcanium binds its own promoter DNA in a divalent cation-dependent manner

Aerobic Lineage of the Oxidative Stress Response Protein Rubrerythrin Emerged in an Ancient Microaerobic, (Hyper)Thermophilic Environment

Crystallization and preliminary X-ray diffraction analysis of the lactonaseVmoLac fromVulcanisaeta moutnovskia

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