Transcriptome Analyses of Metabolic Enzymes in Thiosulfate- and Hydrogen-Grown<i>Hydrogenobacter thermophilus</i>Cells

Sato, Yuya; Kanbe, Haruna; Miyano, Hirosuke; Sambongi, Yoshihiro; Arai, Hiroyuki; Ishii, Masaharu; Igarashi, Yasuo

doi:10.1271/bbb.120210

Cited by 7 publications

(7 citation statements)

References 33 publications

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“…Although haloarchaeal pNARs are supposed to form a supercomplex with the Rieske protein and diheme cytochrome b (Yoshimatsu et al ., ; Martinez‐Espinosa et al ., ), H. thermophilus genome contains no homologs of these haloarchaeal genes. H. thermophilus oxidizes hydrogen as the energy source, and previous studies identified membrane‐bound hydrogenases (Ishii et al ., ; Ueda et al ., ; Sato et al ., ) that transfer electron to methionaquinone in this bacterium (Ishii et al ., ). In addition, H. thermophilus conserves genes encoding the respiratory complex I, and the electron transfer from NADH to ubiquinone was observed in a relative species (Scheide et al ., ).…”

Section: Discussionmentioning

confidence: 99%

“…The cells were harvested when the optical density reached 0.5. RNA was extracted from the harvested cells, followed by tiling microarray analysis according to NimbleGen Arrays User's Guide for Gene Expression Analysis (Roche NimbleGen, Basel, Switzerland) as described previously (Sato et al, 2012b). All expression data are deposited in the GEO database under the series accession number of GSE70944.…”

Section: Transcriptomic Analysismentioning

confidence: 99%

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Nitrate reductases in Hydrogenobacter thermophilus with evolutionarily ancient features: distinctive localization and electron transfer

Kameya

Kanbe

Igarashi

et al. 2017

Molecular Microbiology

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Dissimilatory nitrate reductase (NAR) and assimilatory nitrate reductase (NAS) serve as key enzymes for nitrogen catabolism and anabolism in many organisms. We purified NAR and NAS from H. thermophilus, a hydrogen-oxidizing chemolithoautotroph belonging to the phylogenetically deepest branch in the Bacteria domain. Physiological contribution of these enzymes to nitrate respiration and assimilation was clarified by transcriptomic analysis and gene disruption experiments. These enzymes showed several features unreported in bacteria, such as the periplasmic orientation of NAR anchored with a putative transmembrane subunit and the specific electron transfer from a [4Fe-4S]-type ferredoxin to NAS. While some of their enzymatic properties are shared with NARs from archaea and with NASs from phototrophs, phylogenetic analysis indicated that H. thermophilus NAR and NAS have deep evolutionary origins that cannot be explained by a recent horizontal gene transfer event from archaea and phototrophs. These findings revealed the diversity of NAR and NAS in nonphotosynthetic bacteria, and they also implied that the outward orientation of NAR and the ferredoxin-dependent electron transfer of NAS are evolutionarily ancient features preserved in H. thermophilus.

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Section: Discussionmentioning

confidence: 99%

Section: Transcriptomic Analysismentioning

confidence: 99%

Nitrate reductases in Hydrogenobacter thermophilus with evolutionarily ancient features: distinctive localization and electron transfer

Kameya

Kanbe

Igarashi

et al. 2017

Molecular Microbiology

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“…Total RNA was extracted from triplicate samples from cultures by the hot-phenol method as previously described 45 or from the midgut symbiont cells by using RNAiso Plus (Takara Bi, Kusatsu, Shiga, Japan) and the RNeasy mini kit (Qiagen). The extracted total RNA was purified by phenol–chloroform extraction and digestion by DNase (RQ1 RNase-Free DNase, Promega, Fitchburg, WI, USA) and repurified by using a RNeasy Mini Kit.…”

Section: Methodsmentioning

confidence: 99%

Insecticide resistance by a host-symbiont reciprocal detoxification

et al. 2021

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Insecticide resistance is one of the most serious problems in contemporary agriculture and public health. Although recent studies revealed that insect gut symbionts contribute to resistance, the symbiont-mediated detoxification process remains unclear. Here we report the in vivo detoxification process of an organophosphorus insecticide, fenitrothion, in the bean bug Riptortus pedestris. Using transcriptomics and reverse genetics, we reveal that gut symbiotic bacteria degrade this insecticide through a horizontally acquired insecticide-degrading enzyme into the non-insecticidal but bactericidal compound 3-methyl-4-nitrophenol, which is subsequently excreted by the host insect. This integrated “host-symbiont reciprocal detoxification relay” enables the simultaneous maintenance of symbiosis and efficient insecticide degradation. We also find that the symbiont-mediated detoxification process is analogous to the insect genome-encoded fenitrothion detoxification system present in other insects. Our findings highlight the capacity of symbiosis, combined with horizontal gene transfer in the environment, as a powerful strategy for an insect to instantly eliminate a toxic chemical compound, which could play a critical role in the human-pest arms race.

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“…The Sox system, one of the best-characterized pathways, has been investigated in the neutrophilic sulfur bacterium Paracoccus pantotrophus ( Friedrich et al, 2001 ). Sox systems and their related genes are widespread among sulfur-oxidizing bacteria, including both photo- and chemoautotrophs ( Hensen et al, 2006 ; Sato et al, 2012 ). The complete Sox system in P. pantotrophus contains four components: SoxXA, SoxYZ, SoxB, and Sox(CD) 2 .…”

Section: Introductionmentioning

confidence: 99%

Tetrathionate hydrolase from the acidophilic microorganisms

Kanao

2024

Front. Microbiol.

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Tetrathionate hydrolase (TTH) is a unique enzyme found in acidophilic sulfur-oxidizing microorganisms, such as bacteria and archaea. This enzyme catalyzes the hydrolysis of tetrathionate to thiosulfate, elemental sulfur, and sulfate. It is also involved in dissimilatory sulfur oxidation metabolism, the S4-intermediate pathway. TTHs have been purified and characterized from acidophilic autotrophic sulfur-oxidizing microorganisms. All purified TTHs show an optimum pH in the acidic range, suggesting that they are localized in the periplasmic space or outer membrane. In particular, the gene encoding TTH from Acidithiobacillus ferrooxidans (Af-tth) was identified and recombinantly expressed in Escherichia coli cells. TTH activity could be recovered from the recombinant inclusion bodies by acid refolding treatment for crystallization. The mechanism of tetrathionate hydrolysis was then elucidated by X-ray crystal structure analysis. Af-tth is highly expressed in tetrathionate-grown cells but not in iron-grown cells. These unique structural properties, reaction mechanisms, gene expression, and regulatory mechanisms are discussed in this review.

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Transcriptome Analyses of Metabolic Enzymes in Thiosulfate- and Hydrogen-GrownHydrogenobacter thermophilusCells

Cited by 7 publications

References 33 publications

Nitrate reductases in Hydrogenobacter thermophilus with evolutionarily ancient features: distinctive localization and electron transfer

Nitrate reductases in Hydrogenobacter thermophilus with evolutionarily ancient features: distinctive localization and electron transfer

Insecticide resistance by a host-symbiont reciprocal detoxification

Tetrathionate hydrolase from the acidophilic microorganisms

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