Journal Article
- Thermococcus indicus sp. nov., a Fe(III)-reducing hyperthermophilic archaeon isolated from the Onnuri Vent Field of the Central Indian Ocean ridge
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Jae Kyu Lim , Yun Jae Kim , Jhung-Ahn Yang , Teddy Namirimu , Sung-Hyun Yang , Mi-Jeong Park , Yong Min Kwon , Hyun Sook Lee , Sung Gyun Kang , Jung-Hyun Lee , Kae Kyoung Kwon
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J. Microbiol. 2020;58(4):260-267. Published online April 1, 2020
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DOI: https://doi.org/10.1007/s12275-020-9424-9
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Abstract
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A strictly anaerobic, dissimilatory Fe(III)-reducing hyperthermophilic
archaeon, designated as strain IOH1T, was isolated
from a new deep-sea hydrothermal vent (Onnuri Vent Field)
area in the Central Indian Ocean ridge. Strain IOH1T showed
> 99% 16S rRNA gene sequence similarity with Thermococcus
celericrescens TS2T (99.4%) and T. siculi DSM 12349T (99.2%).
Additional three species T. barossii SHCK-94T (99.0%), T. celer
Vu13T (98.8%), and T. piezophilus (98.6%) showed > 98.6%
of 16S rRNA gene sequence similarity, however, the maximum
OrthoANI value is 89.8% for the genome of T. celericrescens
TS2T. Strain IOH1T cells are coccoid, 1.2–1.8 μm
in diameter, and motile by flagella. Growth was at 70–82°C
(optimum 80°C), pH 5.4–8.0 (optimum pH 6.0) with 2–4%
(optimum 3%) NaCl. Growth of strain IOH1T was enhanced
by starch, pyruvate, D(+)-maltose and maltodextrin as a carbon
sources, and elemental sulfur as an electron acceptor;
clearly different from those of related species T. celecrescens
DSM 17994T and T. siculi DSM 12349T. Strain IOH1T, T. celercrescence
DSM 17994T, and T. siculi DSM 12349T reduced
soluble Fe(III)-citrate present in the medium, whereas the
amount of total cellular proteins increased with the concomitant
accumulation of Fe(II). We determined a circular chromosome
of 2,234 kb with an extra-chromosomal archaeal
plasmid, pTI1, of 7.7 kb and predicted 2,425 genes. The DNA
G + C content was 54.9 mol%. Based on physiological properties,
phylogenetic, and genome analysis, we proposed that
strain IOH1T (= KCTC 15844T = JCM 39077T) is assigned to
a new species in the genus Thermococcus and named Thermococcus
indicus sp. nov.
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Citations
Citations to this article as recorded by

- Macrobenthic communities in the polymetallic nodule field, Indian Ocean, based on multicore and box core analysis
Santosh Gaikwad, Sabyasachi Sautya, Samir Damare, Maria Brenda Luzia Mascarenhas-Pereira, Vijayshree Gawas, Jayesh Patil, Mandar Nanajkar, Sadiq Bukhari
Frontiers in Marine Science.2024;[Epub] CrossRef -
Thermococcus argininiproducens sp. nov., an arginine biosynthesis archaeal species isolated from the Central Indian Ocean ridge
Yeong-Jun Park, Jae Kyu Lim, Yun Jae Kim, Sung-Hyun Yang, Hyun Sook Lee, Sung Gyun Kang, Jung-Hyun Lee, Youngik Yang, Kae Kyoung Kwon
International Journal of Systematic and Evolutionary Microbiology
.2023;[Epub] CrossRef - Spatial comparison and temporal evolution of two marine iron-rich microbial mats from the Lucky Strike Hydrothermal Field, related to environmental variations
Aina Astorch-Cardona, Mathilde Guerre, Alain Dolla, Valérie Chavagnac, Céline Rommevaux
Frontiers in Marine Science.2023;[Epub] CrossRef - Formate and hydrogen in hydrothermal vents and their use by extremely thermophilic methanogens and heterotrophs
James F. Holden, Harita Sistu
Frontiers in Microbiology.2023;[Epub] CrossRef - Microbiome and environmental adaption mechanisms in deep-sea hydrothermal vents
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International Journal of Systematic and Evolutionary Microbiology
.2021;[Epub] CrossRef - Thermococcus aciditolerans sp. nov., a piezotolerant, hyperthermophilic archaeon isolated from a deep-sea hydrothermal vent chimney in the Southwest Indian Ridge
Xue-Gong Li, Hong-Zhi Tang, Wei-Jia Zhang, Xiao-Qing Qi, Zhi-Guo Qu, Jun Xu, Long-Fei Wu
International Journal of Systematic and Evolutionary Microbiology.2021;[Epub] CrossRef - Microorganisms from deep-sea hydrothermal vents
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Marine Life Science & Technology.2021; 3(2): 204. CrossRef
Research Support, Non-U.S. Gov't
- Identification of an Extracellular Thermostable Glycosyl Hydrolase Family 13 α-Amylase from Thermotoga neapolitana
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Kyoung-Hwa Choi , Sungmin Hwang , Hee-Seob Lee , Jaeho Cha
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J. Microbiol. 2011;49(4):628-634. Published online September 2, 2011
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DOI: https://doi.org/10.1007/s12275-011-0432-7
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Scopus
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Abstract
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We cloned the gene for an extracellular α-amylase, AmyE, from the hyperthermophilic bacterium Thermotoga
neapolitana and expressed it in Escherichia coli. The molecular mass of the enzyme was 92 kDa as a monomer.
Maximum activity was observed at pH 6.5 and temperature 75°C and the enzyme was highly thermostable.
AmyE hydrolyzed the typical substrates for α-amylase, including soluble starch, amylopectin, and maltooligosaccharides.
The hydrolytic pattern of AmyE was similar to that of a typical α-amylase; however, unlike
most of the calcium (Ca2+)-dependent α-amylases, the activity of AmyE was unaffected by Ca2+. The specific
activities of AmyE towards various substrates indicated that the enzyme preferred maltooligosaccharides
which have more than four glucose residues. AmyE could not hydrolyze maltose and maltotriose. When
maltoheptaose was incubated with AmyE at the various time courses, the products consisting of maltose
through maltopentaose was evenly formed indicating that the enzyme acts in an endo-fashion. The specific
activity of AmyE (7.4 U/mg at 75°C, pH 6.5, with starch as the substrate) was extremely lower than that
of other extracellular α-amylases, which indicates that AmyE may cooperate with other highly active extracellular
α-amylases for the breakdown of the starch or α-glucans into maltose and maltotriose before transport
into the cell in the members of Thermotoga sp.
Review
- REVIEW] The Linkage between Reverse Gyrase and Hyperthermophiles: A Review of Their Invariable Association
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Michelle Heine , Sathees B.C. Chandra
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J. Microbiol. 2009;47(3):229-234. Published online June 26, 2009
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DOI: https://doi.org/10.1007/s12275-009-0019-8
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Abstract
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With the discovery of reverse gyrase in 1972, from Yellowstone National Park, isolated from Sulfolobus acidocaldarius, it has been speculated as to why reverse gyrase can be found in all hyperthermophiles and just what exactly its role is in hyperthermophilic organisms. Hyperthermophiles have been defined as organisms with an optimal growth temperature of above 85°C. Reverse gyrase is responsible for the introduction of positive supercoils into closed circular DNA. This review of reverse gyrase in hyperthermophilic microorganisms summarizes the last two decades of research performed on hyperthermophiles and reverse gyrase in an effort to provide an up to date synopsis of their invariable association. From the data gathered for this review it is reasonable to hypothesize that reverse gyrase is closely tied to hyperthermophilic life.