• Journal of Microbiology and Biotechnology
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• 제4권1호
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• pp.36-40
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• 1994

A water sample was taken from a black smoker chimney of a deep-sea hydrothermal vent by using an unmanned submersible "Dolphin 3K". The temperature of the hydrothermal fluid from the black smoker was $276^{\circ}C$. After isolation by repeated serial dilutions, An extremely thermophilic bacterial strain was selected. The strain designated as DT1331, was an anaerobic, non-motile, coccoid shaped bacterium with about 0.5 to $1.0\;\mu\textrm{m}$ in diameter. The strain DT1331 could grow up to $93^{\circ}C$, but the optimum temperature of this strain was $80^{\circ}C$. The growth occurred in the pH range of 4.5 to 8.5 and the optimum pH was 6.0. The strain DT1331 required 1% to 5% NaCl for growth and cell lysis was observed below 1% NaCl concentration. The bacterium could grow on polypeptides such as tryptone, peptone, soytone and on proteins such as casein or gelatin. However, no growth was observed on single amino acids, sugar and organic acids. Hydrogen gas was detected slightly during growth. This bacterium obligately required elemental sulfur and hydrogen sulfide gas was produced during growth.

• Molecules and Cells
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• 제24권3호
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• pp.437-440
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• 2007

$OGL-20P^T$-358 is a novel 66 amino acid residue protein from the hyperthermophile Thermococcus thioreducens sp. nov., strain $OGL-20P^T$, which was collected from the wall of the hydrothermal black smoker in the Rainbow Vent along the mid-Atlantic ridge. This protein, which has no detectable sequence homology with proteins or domains of known function, has a calculated pI of 4.76 and a molecular mass of 8.2 kDa. We report here the backbone $^1H$, $^{15}N$, and $^{13}C$ resonance assignments of $OGL-20P^T$-358. Assignments are 97.5% (316/324) complete. Chemical shift index was used to determine the secondary structure of the protein, which appears to consist of primarily ${\alpha}$-helical regions. This work is the foundation for future studies to determine the three-dimensional solution structure of the protein.