Complete genome sequence of hyperthermophilic archaeon Thermococcus sp. ES1

Jung, Jong‐Hyun; Kim, You‐Tae; Jeon, Eun-Jung; Seo, Dong-Ho; Hensley, Sarah A.; Holden, James F.; Lee, Ju-Hoon; Park, Cheon-Seok

doi:10.1016/j.jbiotec.2014.01.022

Cited by 7 publications

(12 citation statements)

References 16 publications

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“…). Alternatively, T. paralvinellae has gene homologs for a soluble, Fd‐dependent formate dehydrogenase (Jung et al ., ), but there was no increase in expression of these genes with added H 2 , and previous Fd‐dependent formate dehydrogenase enzyme activity assays using T. paralvinellae showed no activity (Hensley et al ., ). In E. coli , formate and acetyl‐CoA are made from pyruvate by pyruvate formate lyase (PFL) when the disposal of electrons on NADH is inhibited (Fig.…”

Section: Resultsmentioning

confidence: 73%

“…In Thermococcus , pyruvate cleavage and oxidation are catalyzed by pyruvate oxidoreductase and are Fd dependent rather than NAD + dependent. There is no bacterial PFL homolog in T. paralvinellae (Jung et al ., ) and there was no evidence for this enzyme activity in T. zilligii or T. litoralis that produced formate (Xavier et al ., ; Takács et al ., ).…”

Section: Resultsmentioning

confidence: 99%

“…This suggests that other hydrogenases were active in T. paralvinellae under the same growth conditions. P. furiosus has one Mbh and two SH (Schut et al ., ) while the T. paralvinellae genome contains seven hydrogenase operons: two fhl s, two mbh s, a codh , a sh and a frh (Supporting Information Table S1) (Jung et al ., ).…”

Section: Introductionmentioning

confidence: 97%

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Formate hydrogenlyase and formate secretion ameliorate H₂ inhibition in the hyperthermophilic archaeon Thermococcus paralvinellae

Topçuoğlu

Meydan

Orellana

et al. 2017

Environmental Microbiology

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Some hyperthermophilic heterotrophs in the genus Thermococcus produce H in the absence of S° and have up to seven hydrogenases, but their combined physiological roles are unclear. Here, we show which hydrogenases in Thermococcus paralvinellae are affected by added H during growth without S°. Growth rates and steady-state cell concentrations decreased while formate production rates increased when T. paralvinallae was grown in a chemostat with 65 µM of added H . Differential gene expression analysis using RNA-Seq showed consistent expression of six hydrogenase operons with and without added H . In contrast, expression of the formate hydrogenlyase 1 (fhl1) operon increased with added H . Flux balance analysis showed H oxidation and formate production using FHL became an alternate route for electron disposal during H inhibition with a concomitant increase in growth rate relative to cells without FHL. T. paralvinellae also grew on formate with an increase in H production rate relative to growth on maltose or tryptone. Growth on formate increased fhl1 expression but decreased expression of all other hydrogenases. Therefore, Thermococcus that possess fhl1 have a competitive advantage over other Thermococcus species in hot subsurface environments where organic substrates are present, S° is absent and slow H efflux causes growth inhibition.

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Section: Resultsmentioning

confidence: 73%

Section: Resultsmentioning

confidence: 99%

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Formate hydrogenlyase and formate secretion ameliorate H₂ inhibition in the hyperthermophilic archaeon Thermococcus paralvinellae

Topçuoğlu

Meydan

Orellana

et al. 2017

Environmental Microbiology

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“…A gene cluster similar to that of T. kodakarensis has been found in other Thermococcus strain. Thermococcus paralvinellae is the only organism that has a gene cluster composed of 14 genes (TES1_0498 to TES1_0511) including the argG, argH, carA, and carB homologs in 13 Thermococcus strains in the KEGG database (19) (Fig. 11).…”

Section: Discussionmentioning

confidence: 99%

Lysine Biosynthesis of Thermococcus kodakarensis with the Capacity to Function as an Ornithine Biosynthetic System

Yoshida

Tanaka

Atomi

et al. 2016

Journal of Biological Chemistry

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We recently discovered a biosynthetic system using a novel amino group carrier protein called LysW for lysine biosynthesis via α-aminoadipate (AAA), and revealed that this system is also utilized in the biosynthesis of arginine by Sulfolobus In the present study, we focused on the biosynthesis of lysine and ornithine in the hyperthermophilic archaeon Thermococcus kodakarensis, and showed that their biosynthesis is accomplished by a single set of metabolic enzymes. We also determined the crystal structure of the LysX family protein from T. kodakarensis, which catalyzes the conjugation of LysW with either AAA or glutamate, in a complex with LysW-γ-AAA. This crystal structure is the first example to show how LysX recognizes AAA as a substrate and provides a structural basis for the bifunctionality of the LysX family protein from T. kodakarensis Based on comparisons with other LysX family proteins, we propose a mechanism for substrate recognition and its relationship with molecular evolution among LysX family proteins, which have different substrate specificities.

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“…Thermococcus paralvinellae produced H 2 when grown on both maltose and tryptone (0.5% wt vol −1 of each) without sulfur (Hensley et al, 2014 ). Its complete genome sequence contains seven hydrogenase gene clusters (Jung et al, 2014 ). Four of these clusters are putatively membrane bound and use ferredoxin, formate and CO as electron donors coupled with H + /Na + translocation, and three are cytoplasmic and use NAD(P)H or coenzyme F 420 as electron pairs (Figure 1 ).…”

Section: Introductionmentioning

confidence: 99%

Hydrogen Production and Enzyme Activities in the Hyperthermophile Thermococcus paralvinellae Grown on Maltose, Tryptone, and Agricultural Waste

2016

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Thermococcus may be an important alternative source of H2 in the hot subseafloor in otherwise low H2 environments such as some hydrothermal vents and oil reservoirs. It may also be useful in industry for rapid agricultural waste treatment and concomitant H2 production. Thermococcus paralvinellae grown at 82°C without sulfur produced up to 5 mmol of H2 L−1 at rates of 5–36 fmol H2 cell−1 h−1 on 0.5% (wt vol−1) maltose, 0.5% (wt vol−1) tryptone, and 0.5% maltose + 0.05% tryptone media. Two potentially inhibiting conditions, the presence of 10 mM acetate and low pH (pH 5) in maltose-only medium, did not significantly affect growth or H2 production. Growth rates, H2 production rates, and cell yields based on H2 production were the same as those for Pyrococcus furiosus grown at 95°C on the same media for comparison. Acetate, butyrate, succinate, isovalerate, and formate were also detected as end products. After 100 h, T. paralvinellae produced up to 5 mmol of H2 L−1 of medium when grown on up to 70% (vol vol−1) waste milk from cows undergoing treatment for mastitis with the bacterial antibiotic Ceftiofur and from untreated cows. The amount of H2 produced by T. paralvinellae increased with increasing waste concentrations, but decreased in P. furiosus cultures supplemented with waste milk above 1% concentration. All mesophilic bacteria from the waste milk that grew on Luria Bertani, Sheep's Blood (selective for Staphylococcus, the typical cause of mastitis), and MacConkey (selective for Gram-negative enteric bacteria) agar plates were killed by heat during incubation at 82°C. Ceftiofur, which is heat labile, was below the detection limit following incubation at 82°C. T. paralvinellae also produced up to 6 mmol of H2 L−1 of medium when grown on 0.1–10% (wt vol−1) spent brewery grain while P. furiosus produced < 1 mmol of H2 L−1. Twelve of 13 enzyme activities in T. paralvinellae showed significant (p < 0.05) differences across six different growth conditions; however, methyl viologen-dependent membrane hydrogenase activity remained constant across all media types. The results demonstrate the potential of at least some Thermococcus species to produce H2 if protein and α-glucosides are present as substrates.

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Complete genome sequence of hyperthermophilic archaeon Thermococcus sp. ES1

Cited by 7 publications

References 16 publications

Formate hydrogenlyase and formate secretion ameliorate H₂ inhibition in the hyperthermophilic archaeon Thermococcus paralvinellae

Formate hydrogenlyase and formate secretion ameliorate H₂ inhibition in the hyperthermophilic archaeon Thermococcus paralvinellae

Lysine Biosynthesis of Thermococcus kodakarensis with the Capacity to Function as an Ornithine Biosynthetic System

Hydrogen Production and Enzyme Activities in the Hyperthermophile Thermococcus paralvinellae Grown on Maltose, Tryptone, and Agricultural Waste

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Complete genome sequence of hyperthermophilic archaeon Thermococcus sp. ES1

Cited by 7 publications

References 16 publications

Formate hydrogenlyase and formate secretion ameliorate H2 inhibition in the hyperthermophilic archaeon Thermococcus paralvinellae

Formate hydrogenlyase and formate secretion ameliorate H2 inhibition in the hyperthermophilic archaeon Thermococcus paralvinellae

Lysine Biosynthesis of Thermococcus kodakarensis with the Capacity to Function as an Ornithine Biosynthetic System

Hydrogen Production and Enzyme Activities in the Hyperthermophile Thermococcus paralvinellae Grown on Maltose, Tryptone, and Agricultural Waste

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Formate hydrogenlyase and formate secretion ameliorate H₂ inhibition in the hyperthermophilic archaeon Thermococcus paralvinellae

Formate hydrogenlyase and formate secretion ameliorate H₂ inhibition in the hyperthermophilic archaeon Thermococcus paralvinellae