Genome Sequence of a Hyperthermophilic Archaeon, Thermococcus nautili 30-1, That Produces Viral Vesicles

Oberto, Jacques; Gaudin, Marie; Cossu, Matteo; Gorlas, Aurore; Slesarev, Alexei I.; Marguet, Evelyne; Forterre, Patrick

doi:10.1128/genomea.00243-14

Cited by 12 publications

(12 citation statements)

References 23 publications

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“…To determine if our model Thermococcus species, Thermococcus nautili [37] , [38] also produces sulfur vesicles, we examined T. nautili cells directly by Cryo-EM. As expected, Fig.…”

Section: Resultsmentioning

confidence: 99%

Sulfur vesicles from Thermococcales: A possible role in sulfur detoxifying mechanisms

et al. 2015

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The euryarchaeon Thermococcus prieurii inhabits deep-sea hydrothermal vents, one of the most extreme environments on Earth, which is reduced and enriched with heavy metals. Transmission electron microscopy and cryo-electron microscopy imaging of T. prieurii revealed the production of a plethora of diverse membrane vesicles (MVs) (from 50 nm to 400 nm), as is the case for other Thermococcales. T. prieurii also produces particularly long nanopods/nanotubes, some of them containing more than 35 vesicles encased in a S-layer coat. Notably, cryo-electron microscopy of T. prieurii cells revealed the presence of numerous intracellular dark vesicles that bud from the host cells via interaction with the cytoplasmic membrane. These dark vesicles are exclusively found in conjunction with T. prieurii cells and never observed in the purified membrane vesicles preparations. Energy-Dispersive-X-Ray analyses revealed that these dark vesicles are filled with sulfur. Furthermore, the presence of these sulfur vesicles (SVs) is exclusively observed when elemental sulfur was added into the growth medium. In this report, we suggest that these atypical vesicles sequester the excess sulfur not used for growth, thus preventing the accumulation of toxic levels of sulfur in the host's cytoplasm. These SVs transport elemental sulfur out of the cell where they are rapidly degraded. Intriguingly, closely related archaeal species, Thermococcus nautili and Thermococcus kodakaraensis, show some differences about the production of sulfur vesicles. Whereas T. kodakaraensis produces less sulfur vesicles than T. prieurii, T. nautili does not produce such sulfur vesicles, suggesting that Thermococcales species exhibit significant differences in their sulfur metabolic pathways.

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“…To determine if our model Thermococcus species, Thermococcus nautili [37] , [38] also produces sulfur vesicles, we examined T. nautili cells directly by Cryo-EM. As expected, Fig.…”

Section: Resultsmentioning

confidence: 99%

Sulfur vesicles from Thermococcales: A possible role in sulfur detoxifying mechanisms

et al. 2015

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“…Moreover, NSun6 homologs are conserved in other hyperthermophilic archaea, such as Pyrococcus kukulkanii NCB100 (35), Pyrococcus abyssi GE5 (http://www.genoscope.cns.fr/Pab/), Thermococcus litoralis NS-C (36) and Thermococcus nautili 30-1 (37). These archaeal NSun6 homologs all share identity with PH1991 (Supplementary Figure S1).…”

Section: Introductionmentioning

confidence: 99%

Archaeal NSUN6 catalyzes m5C72 modification on a wide-range of specific tRNAs

Long

et al. 2018

Nucleic Acids Research

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Human NOL1/NOP2/Sun RNA methyltransferase family member 6 (hNSun6) generates 5-methylcytosine (m 5 C) at C72 of four specific tRNAs, and its homologs are present only in higher eukaryotes and hyperthermophilic archaea. Archaeal NSun6 homologs possess conserved catalytic residues, but have distinct differences in their RNA recognition motifs from eukaryotic NSun6s. Until now, the biochemical properties and functions of archaeal NSun6 homologs were unknown. In archaeon Pyrococcus horikoshii OT3, the gene encoding the NSun6 homolog is PH1991 . We demonstrated that the PH1991 protein could catalyze m 5 C72 formation on some specific Ph tRNAs in vitro and was thus named as Ph NSun6. Remarkably, Ph NSun6 has a much wider range of tRNA substrates than hNSun6, which was attributed to its tRNA substrate specificity. The mechanism was further elucidated using biochemical and crystallographic experiments. Structurally, the binding pocket for nucleotide 73 in Ph NSun6 is specific to accommodate U73 or G73-containing Ph tRNAs. Furthermore, Ph NSun6 lacks the eukaryotic NSun6-specific Lys-rich loop, resulting in the non-recognition of D-stem region by Ph NSun6. Functionally, the m 5 C72 modification could slightly promote the thermal stability of Ph tRNAs, but did not affect the amino acid accepting activity of Ph tRNAs.

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“…sp. EXT12c is most closely related to T. nautili strain 30-1 T ( 16 ). These genomes have a DNA-DNA hybridization value of 43.6% and an average nucleotide identity of 91.18%, as predicted with GGDC v2.1 ( 17 – 19 ) and OrthoANI v1.20 ( 20 ), respectively.…”

Section: Genome Announcementmentioning

confidence: 99%

Complete Genome Sequence of Hyperthermophilic Archaeon Thermococcus sp. EXT12c, Isolated from the East Pacific Rise 9°N

et al. 2017

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Genome Sequence of a Hyperthermophilic Archaeon, Thermococcus nautili 30-1, That Produces Viral Vesicles

Cited by 12 publications

References 23 publications

Sulfur vesicles from Thermococcales: A possible role in sulfur detoxifying mechanisms

Sulfur vesicles from Thermococcales: A possible role in sulfur detoxifying mechanisms

Archaeal NSUN6 catalyzes m5C72 modification on a wide-range of specific tRNAs

Complete Genome Sequence of Hyperthermophilic Archaeon Thermococcus sp. EXT12c, Isolated from the East Pacific Rise 9°N

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