Tairo Oshima

ORCID: 0000-0001-8576-9422
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About
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Research Areas
  • Enzyme Structure and Function
  • RNA and protein synthesis mechanisms
  • Polyamine Metabolism and Applications
  • Protein Structure and Dynamics
  • Amino Acid Enzymes and Metabolism
  • Biochemical and Molecular Research
  • Genomics and Phylogenetic Studies
  • Bacteriophages and microbial interactions
  • RNA modifications and cancer
  • Photosynthetic Processes and Mechanisms
  • Mass Spectrometry Techniques and Applications
  • Microbial Metabolic Engineering and Bioproduction
  • Enzyme Catalysis and Immobilization
  • DNA and Nucleic Acid Chemistry
  • Hemoglobin structure and function
  • Metabolism and Genetic Disorders
  • Metalloenzymes and iron-sulfur proteins
  • ATP Synthase and ATPases Research
  • Photoreceptor and optogenetics research
  • Origins and Evolution of Life
  • Microbial Community Ecology and Physiology
  • Enzyme Production and Characterization
  • Biopolymer Synthesis and Applications
  • Bacterial Genetics and Biotechnology
  • Space Science and Extraterrestrial Life

Kyowa-kako (Japan)
2013-2023

Chiba Institute of Science
2023

ENVIRON (United States)
2015

Kyushu University
2012

Tokyo University of Pharmacy and Life Sciences
2001-2011

Chiba Institute of Technology
2009

Institute of Microbiology
2005-2007

Tokyo Institute of Technology
1992-2005

The University of Tokyo
1975-2003

Kyoto University Institute for Chemical Research
1997

Active transport across the vacuolar components of eukaryotic endomembrane system is energized by a specific H+-ATPase. The amino acid sequences 70- and 60-kDa subunits H+-ATPase are approximately equal to 25% identical beta alpha subunits, respectively, eubacterial-type F0F1-ATPases. We now report that same 50% sulfur-metabolizing Sulfolobus acidocaldarius, an archaebacterium (Archaeobacterium). Moreover, homologue 88-amino stretch near amino-terminal end 70-kDa subunit absent from...

10.1073/pnas.86.17.6661 article EN Proceedings of the National Academy of Sciences 1989-09-01

The properties of an extremely thermophilic bacterium isolated from water at a Japanese hot spring and previously named Flavobacterium thermophilum are described. cells gram-negative, nonsporulating, aerobic rods containing yellow pigment. optimum temperature for growth is between 65 72 C, the maximum being 85 C minimum 47 C. guanine plus cytosine content deoxyribonucleic acid thermophile 69 mol %. This microorganism sensitive to various antibiotics including those which known be rather...

10.1099/00207713-24-1-102 article EN International Journal of Systematic Bacteriology 1974-01-01

Emerging X-ray free-electron lasers with femtosecond pulse duration enable single-shot snapshot imaging almost free from sample damage by outrunning major radiation processes. In bioimaging, it is essential to keep the close its natural state. Conventional high-resolution imaging, however, suffers severe that hinders live cell imaging. Here we present a method for capturing snapshots of cells kept in micro-liquid enclosure array laser diffraction. We place living Microbacterium lacticum an...

10.1038/ncomms4052 article EN cc-by-nc-nd Nature Communications 2014-01-07

In studies on the cause of extreme stability macromolecules Thermus thermophilwr HB8, leuB gene coding for 3-isopropylmalate dehydrogenase leucine synthesis pathway and its flanking regions were cloned sequenced.The T. thermophilus was expressed in a leuB-less mutant Escherichia coli, thermostable purified from an extract cells.The primary structure thermophilic isopropylmalate deduced nucleotide sequence (1017 base pairs) amino acid peptides isolated dehydrogenase.The has M, = 35,968, value...

10.1016/s0021-9258(17)43242-x article EN cc-by Journal of Biological Chemistry 1984-03-01

Knots in polypeptide chains have been found very few proteins. Only two proteins are considered to a shallow `trefoil' knot, which tucks residues at one end of the chain through loop exposed on protein surface. Recently, another was by mathematical algorithm deep `figure-of-eight' knot had not visually identified. In present study, crystal structure hypothetical RNA 2′-O-ribose methyltransferase from Thermus thermophilus (RrmA) determined 2.4 Å resolution and trefoil for first time. The is...

10.1107/s0907444902006601 article EN Acta Crystallographica Section D Biological Crystallography 2002-06-20

The gene of an extreme thermophile, Thermus thermophilus HB8, which codes for a leucine biosynthetic enzyme, 3-isopropylmalate (3-IPM) dehydrogenase [EC 1.1.1.85], was cloned in Escherichia coli using pBR322 as vector. E. cells carrying this recombinant plasmid, pHB2, produced the thermophilic enzyme 7-fold more than did T. HB8 cells. When crude extract pHB2-carrying treated at 70 degrees C 10 min, approximately 75% protein precipitated with full activity 3-IPM being left supernatant,...

10.1093/oxfordjournals.jbchem.a133245 article EN The Journal of Biochemistry 1981-01-01

We cloned and sequenced the leuB gene encoding 3‐isopropylmalate dehydrogenase from Escherichia coli K‐12 (JM103). Errors (33 residues) were found corrected in sequence previously reported for of Thermus thermophilus . The three‐dimensional structure thermophile enzyme amino acid comparison suggested that a part high stability T. is conferred by increased hydrophobic interaction at subunit‐subunit interface. Two residues interface enzyme, Leu246 Val249, are substituted with less residues,...

10.1111/j.1432-1033.1994.tb18623.x article EN European Journal of Biochemistry 1994-02-01

Extreme thermophiles produce two types of unusual polyamine: long linear polyamines such as caldopentamine and caldohexamine, branched quaternary ammonium compounds [e.g. tetrakis(3-aminopropyl)ammonium]. To clarify the physiological roles in thermophiles, we synthesized them chemically tested their effects on stability ds (double-stranded) ss (single-stranded) DNAs tRNA response to thermal denaturation, measured by differential scanning calorimetry. Linear stabilized dsDNA proportion number...

10.1042/bj20041778 article EN Biochemical Journal 2005-05-24

Isolation of novel membrane-associated ATPases, presumably soluble parts the H+-ATPases, from archaebacteria has been recently reported, and their properties were found to be significantly different usual F1-ATPase. In order assess relationship archaebacterial ATPases F1-ATPases other known amino acid sequence alpha subunit ATPase Sulfolobus acidocaldarius, an acidothermophilic archaebacterium, was compared with sequences ATPases. The gene encoding its cloned genomic library S. nucleotide...

10.1016/s0021-9258(18)68740-x article EN cc-by Journal of Biological Chemistry 1988-05-01

A bacteriophage (phiYS40) infectious to an extreme thermophile, Thermus thermophilus HB8, was isolated and characterized. phiYS40 grows over the temperature range of 56 78 C, optimum growth is about 65 C. The phage had a latent period 80 min burst size at has hexagonal head 0.125 mum in diameter, tail 0.178 long 0.027 wide, base plate fibers. thermostable broth but rather unstable buffer containing 10 mM Tris, MgCl2, pH 7.5. addition Casamino Acids (1 percent), polypeptone (0.8 yeast extract...

10.1128/jvi.15.6.1449-1453.1975 article EN Journal of Virology 1975-06-01

Thermoplasma acidophilum HO-62 was grown at different pHs and temperatures, its polar lipid compositions were determined. Although the number of cyclopentane rings in caldarchaeol moiety increased when T. cultured high temperature, decreased low pHs. Glycolipids, phosphoglycolipids, phospholipids analyzed by high-performance liquid chromatography with an evaporative light-scattering detector. The amount more than two sugar units on one side under low-pH high-temperature conditions. amounts...

10.1128/jb.00415-08 article EN Journal of Bacteriology 2008-06-07

An extreme thermophile has been isolated from a Japanese thermal spa.To elucidate the molecular basis of thermophily, chemical and physical natures cell constituents microorganism are under investigation.In this communication bacterial properties heat stability t-RNA ribosomes will be described.Aliquots (about 2 ml) water sampled hot spring at Mine Hot Spring, Shizuoka, ,Japan, were transferred into polypeptone-yeast extract-sodium chloride media (final 8, 4, 3%) pH 7.0, incubated 75°.The...

10.2323/jgam.17.513 article EN The Journal of General and Applied Microbiology 1971-01-01

The complete nucleotide sequences of the mitochondrial (mt) genomes three cephalopods, Octopus vulgaris (Octopodiformes, Octopoda, Incirrata), Todarodes pacificus (Decapodiformes, Oegopsida, Ommastrephidae), and Watasenia scintillans Enoploteuthidae), were determined. These mt encode standard set metazoan genes. However, W. T. share duplications longest noncoding region, cytochrome oxidase subunit genes two ATP synthase genes, tRNA(Asp) gene. Southern hybridization analysis genome shows that...

10.1093/molbev/msh227 article EN Molecular Biology and Evolution 2004-07-14

The gene which encodes the beta subunit of novel membrane-associated ATPase has been identified and characterized. subunit, is most likely soluble part non-F0F1 type H+-ATPase, was obtained from archaebacterium, Sulfolobus acidocaldarius. In terms its location, it follows just after for alpha subunit. It comprised 1398 nucleotides, corresponding to a protein 465 amino acids, consensus sequence in nucleotide binding proteins poorly conserved. Together with previously described results,...

10.1016/s0021-9258(19)77827-2 article EN cc-by Journal of Biological Chemistry 1988-11-01

An ATPase with Mr of 360,000 was purified from plasma membranes a thermophilic eubacterium Thermus thermophilus, and characterized. ATP hydrolytic activity the enzyme extremely low, 0.07 mumol Pi released mg-1 min-1, it stimulated up to 30-fold by bisulfite. The following properties indicate that is not usual F1-ATPase but belongs V-type family, another class ATPases found in archaebacteria eukaryotic endomembranes. Among its four kinds subunits approximate values 66,000 (alpha), 55,000...

10.1016/s0021-9258(18)45830-9 article EN cc-by Journal of Biological Chemistry 1990-12-01

The catalytic and allosteric sites of proton translocating adenosine triphosphatase (ATPase) were studied by measuring the binding nucleotides to ATPase, its α β subunits purified from thermophilic bacterium PS3, with a circular dichroic spectrometer. In contrast mesophilic ATPases, this enzyme contained no tightly bound nucleotides, stable after their purification. These properties advantageous for analyzing both sites. former site showed rapid loose binding, but latter slow (t1/2≒1 h, ADP)...

10.1093/oxfordjournals.jbchem.a132904 article EN The Journal of Biochemistry 1980-04-01

Abstract A new polyamine has been extracted from an extreme thermophile, Thermus thermophilus, and its chemical structure was determined as 1,12-diamino-4,8-diazadodecane, NH2(CH2)3NH(CH2)3NH(CH2)4NH2, based on proton NMR, 13C mass spectra. trivial name thermospermine is proposed for the compound.

10.1016/s0021-9258(19)86752-2 article EN cc-by Journal of Biological Chemistry 1979-09-01
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