Yoshiko Nomura

Kyoto University, Kyoto, Kyoto-fu, Japan

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Publications (2)1.79 Total impact

  • [Show abstract] [Hide abstract]
    ABSTRACT: The aerobic hyperthermophilic archaeon Aeropyrum pernix expresses molybdopterin carbon monoxide dehydrogenase (Mo-CODH). A. pernix strains isolated from Tachibana Bay (TB1–8) were found to exhibit different levels of total Mo-CODH activity (low and high, respectively), and the Mo-CODHs isolated from these strains also exhibit high or low activity. Mo-CODH gene transcription was detected by real-time reverse transcription-PCR, but no relation was found between the expression level of mRNA and the activity level of Mo-CODH. The nucleotide sequences of A. pernix genes encoding the small, large, and medium subunits of Mo-CODH, respectively, and those of the putative promoter region were identified from all TB strains. Amino acid substitutions were found in the sequences of high- and low-activity strains, but no mutation was detected in the putative promoter regions. Homology modeling revealed that all amino acid substitutions were localized on the surface of the Mo-CODH proteins. Based on these findings, we conclude that in A. pernix, the activity level of Mo-CODH may be regulated by translation or post-translational modification rather than by genomic diversity or transcription. KeywordsCarbon monoxide dehydrogenase–Aerobe–Hyperthermophile– Aeropyrum –Crenarchaeota–Molybdopterin hydroxylase
    Fisheries Science 01/2011; 77(1):135-141. · 0.90 Impact Factor
  • [Show abstract] [Hide abstract]
    ABSTRACT: The aerobic hyperthermophilic archaeon Aeropyrum pernix expresses carbon monoxide (CO) oxidation activity under heterotrophic growth conditions. Using activity stain gel analysis, CO oxidation activity was detected in a protein with a molecular mass of 210kDa. The 210kDa CODH protein was purified to homogeneity from A. pernix. Aeropyrum Mo-CODH catalyzed the oxidation of CO with a specific activity of 2.1μmol CO min−1 mg−1 at 95°C, pH 8.0 using methyl viologen as the electron acceptor. The CODH protein showed high oxygen and thermo stability. The protein contains three subunits: L (86.6kDa), M (34.5kDa), and S (12.6kDa), which form the LM2S complex. The molecular mass of the complex was calculated by gel filtration and found to be 163.7kDa. N-terminal amino acid sequencing and peptide mass fingerprinting analysis of the subunits indicated that they corresponded to NP_148462.1, NP_148464.2, and NP_148465.1, and their genes annotated the molybdo iron-sulfur flavoprotein carbon monoxide dehydrogenase S, L, and M subunits, respectively. Phylogenetic analysis revealed that CODH belongs to a novel clade of diverse CODHs. KeywordsAerobic-Hyperthermophilic-Crenarchaeota-Carbon monoxide dehydrogenase-Molybdopterin hydroxylase- Aeropyrum
    Fisheries Science 01/2010; 76(6):999-1006. · 0.90 Impact Factor

Publication Stats

1.79 Total Impact Points

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Institutions

  • 2010–2011
    • Kyoto University
      • Division of Applied Biosciences
      Kyoto, Kyoto-fu, Japan