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SUZUKI Katsuyuki

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FacultyDepartment of Biotechnology and Chemistry / Graduate School of System Enginnering
PositionAssociate Professor
Degree
Commentator Guidehttps://www.kindai.ac.jp/meikan/495-suzuki-katsuyuki.html
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Last Updated :2020/09/03

Education and Career

Education

  •  - 1985 , Hiroshima University
  •  - 1985 , Hiroshima University, Graduate School, Division of Engineering
  •  - 1980 , Hiroshima University, Faculty of Engineering
  •  - 1980 , Hiroshima University, Faculty of Engineering

Research Activities

Research Areas

  • Life sciences, Molecular biology
  • Life sciences, Functional biochemistry

Research Interests

  • Functional biochemistry, Molecular Biology

Published Papers

  • Characterization and Radio-resistant Function of Manganese Superoxide Dismutase of Rubrobacter radiotolerans, Hiroaki Terato, Katsuyuki Suzuki, Nobuhiro Nishioka, Atsushi Okamoto, Yuka Shimazaki-Tokuyama, Yuko Inoue, Takeshi Saito, JOURNAL OF RADIATION RESEARCH, JOURNAL OF RADIATION RESEARCH, 52(6), 735 - 742, Nov. 2011
    Summary:Rubrobacter radiotolerans is the most radio-resistant eubacterium without spore-formation in the life cycle, and its D(37) is 16,000 Gy against gamma-rays. To understand the molecular mechanism of the high radio-resistance, we purified and characterized superoxide dismutase (SOD) of this organism as enzymatic radical scavenger, and then analyzed its genetic information. The purified SOD protein formed homotetramerization of 24,000 Da-monomer, while maintaining its enzymatic activity against potassium cyanide and hydrogen peroxide. We obtained a partial amino acid sequence of the protein and cloned the gene from it. Sequence analysis of the cloned gene indicated that the protein showed a similarity to other bacterial manganese SODs (Mn-SODs). Sequencing for adjacent regions of the gene showed that the gene had promoter elements with an open reading frame for putative PAS/PAC sensor protein at the 5'-adjacent region. Introduction of the gene into Escherichia coli cells lacking intrinsic SOD genes restored the cellular enzymatic activity and resistance to methyl viologen, indicating the gene at work. A mutant cell harboring this gene also became resistant against gamma-rays. The present results suggest that the protein in question is the Mn-SOD of R. radiotolerans, a good candidate as a radio-protection factor for this bacterial radio-resistance.
  • A dispensable yeast ribosomal protein optimizes peptidyltransferase activity and affects translocation, J Dresios, P Panopoulos, K Suzuki, D Synetos, JOURNAL OF BIOLOGICAL CHEMISTRY, JOURNAL OF BIOLOGICAL CHEMISTRY, 278(5), 3314 - 3322, Jan. 2003
    Summary:Yeast ribosomal protein L41 is dispensable in the yeast. Its absence had no effect on polyphenylalanine synthesis activity, and a limited effect on growth, translational accuracy, or the resistance toward the antibiotic paromomycin. Removal of L41 did not affect the 60:40 S ratio, but it reduced the amount of 80 S, suggesting that L41 is involved in ribosomal subunit association. However, the two most important effects of L41 were on peptidyltransferase activity and translocation. Peptidyltransferase activity was measured as a second-order rate constant (k(cat)/K-s) corresponding to the rate of peptide bond formation; this k(cat)/K-s was lowered 3-fold to 1.15 min(-1) mM(-1) in the L41 mutant compared with 3.46 min(-1) mM(-1) in the wild type. Translocation was also affected by L41. Elongation factor 2 (EF2)-dependent (enzymatic) translocation of Ac-Phe-tRNA from the A- to P-site was more efficient in the absence of L41, because 50% translocation was achieved at only 0.004 muM EF2 compared with 0.02 muM for the wild type. Furthermore, the EF2-dependent translocation was inhibited by 50% at 2.5 muM of the translocation inhibitor cycloheximide in the L41 mutant compared with 1.2 muM in the wild type. Finally, the rate of EF2-independent (spontaneous) translocation was increased in the absence of L41.
  • Identification of the genes encoding for sigma factors on the genome of alkaliphilic Bacillus halodurans strain C 125, 34, 13 - 16, Dec. 2001
  • Heterogeneity of the genes for 16SrRNA of extremely halophilic triangular archaeon, Haloarcula japonica strain TR 1, 34, 21 - 23, Dec. 2001
  • Cloning and structural analysis of the gene encoding for dihydrofolate dehydrogenase (folA) from shewanella oneidensis, 34, 9 - 11, Dec. 2001
  • Construction of chimeric gene for ntrB of Shewanella violacea and Escherichia coli, 34, 17 - 19, Dec. 2001
  • GPHN, a novel partner gene fused to MLL in a leukemia with t(11;14)(q23;q24), M Eguchi, M Eguchi-Ishimae, M Seto, K Morishita, K Suzuki, R Ueda, K Ueda, N Kamada, M Greaves, GENES CHROMOSOMES & CANCER, GENES CHROMOSOMES & CANCER, 32(3), 212 - 221, Nov. 2001
    Summary:We report a novel MLL-associated chromosome translocation t(11;14)(q23;q24) in a child who showed signs of acute undifferentiated leukemia 3 years after intensive chemotherapy, that included the topoisomerase-II inhibitor VP 16. Screening of a cDNA library of the patient's leukemic cells showed a novel fusion transcript between MLL and the Gephyrin (GPHN) gene on 14q24. The resulting MLL-GPHN fusion gene encodes MLL AT hook motifs and a DNA methyltransferase homology domain fused to the C-terminal half of Gephyrin, including a presumed tubulin binding site and a domain homologous to the Escherichia coli molybdenum cofactor biosynthesis protein MoeA. Genomic breakpoint analysis showed potential, in vitro topoisomerase-II DNA-binding sites spanning the breakpoints in both MLL and GPHN but no flanking sequences that might mediate homologous recombination. This suggests that MLL-GPHN may have been generated by VP 16/topoisomerase-II-induced DNA double-strand breaks, followed by error-prone DNA repair via non-homologous end joining. Gephyrin was originally identified as a submembraneous scaffold protein that anchors and immobilizes postsynaptic membrane neurotransmitter receptors to underlying cytoskeletal elements. It also is reported to bind to phosphatidylinositol 3,4,5-triphosphate binding proteins involved in actin dynamics and downstream signaling and, interacts with ATM-related family member RAFTI. Gephyrin domains in the chimeric protein therefore could contribute novel signal sequences or might modify MLL activity by oligomerization or intracellular redistribution. (C) 2001 Wiley-Liss, Inc.
  • Gene products specifically changée during the sexual response of tremella mesenterica, Katsuyuki Suzuki, Eiko Tsuchiya, Tokichi Miyakawa, Sakuzo Fukui, Agricultural and Biological Chemistry, Agricultural and Biological Chemistry, 49(8), 2471 - 2473, 1985 , Refereed

Books etc

  • Molecular-targeting chemotherapy for gastric cancer. (jointly worked), Progress in Gastric Cancer research in 1997、Eaton Publishing,   1997
  • The evolution of ribosomal proteins and yeast. (jointly worked), Protein Synthesis and Targeting in Yeast, Springer-Verlag/NATO ASI Series,   1993
  • The ribosomal proteins : Compilation of protein species equivalents from various organisms, based on evolutional analyses. (jointly worked), The translational apparatus, Plenum Press,   1993

Conference Activities & Talks

  • In vitro selection of novel DNA aptamers that recognize sacchariaes,   2003 10
  • Structural analysis of the nitrogen fixation-related genes from Paenibacillus ozotofixans,   2002 10
  • Creation of saccharide-binding molecules by combinatorial bio-engineering,   2002 03
  • Stractural analysis of the nitrogen fixation related genes from Paenibacillus azotofixans,   2001 12
  • In vitro selection of DNA aptamer which bind to saccharides,   2001 09
  • In vitro selection of DNA aptamers which bind to saccharides,   2001 03

Misc

  • A dispensable yeast ribosomal protein optimizes peptidyltransferase activity and affects translocation, J Dresios, P Panopoulos, K Suzuki, D Synetos, JOURNAL OF BIOLOGICAL CHEMISTRY, 278, 5, 3314, 3322,   2003 01 , 10.1074/jbc.M207533200
    Summary:Yeast ribosomal protein L41 is dispensable in the yeast. Its absence had no effect on polyphenylalanine synthesis activity, and a limited effect on growth, translational accuracy, or the resistance toward the antibiotic paromomycin. Removal of L41 did not affect the 60:40 S ratio, but it reduced the amount of 80 S, suggesting that L41 is involved in ribosomal subunit association. However, the two most important effects of L41 were on peptidyltransferase activity and translocation. Peptidyltransferase activity was measured as a second-order rate constant (k(cat)/K-s) corresponding to the rate of peptide bond formation; this k(cat)/K-s was lowered 3-fold to 1.15 min(-1) mM(-1) in the L41 mutant compared with 3.46 min(-1) mM(-1) in the wild type. Translocation was also affected by L41. Elongation factor 2 (EF2)-dependent (enzymatic) translocation of Ac-Phe-tRNA from the A- to P-site was more efficient in the absence of L41, because 50% translocation was achieved at only 0.004 muM EF2 compared with 0.02 muM for the wild type. Furthermore, the EF2-dependent translocation was inhibited by 50% at 2.5 muM of the translocation inhibitor cycloheximide in the L41 mutant compared with 1.2 muM in the wild type. Finally, the rate of EF2-independent (spontaneous) translocation was increased in the absence of L41.
  • GPHN, a novel partner gene fused to MLL in a leukemia with t(11;14)(q23;q24), M Eguchi, M Eguchi-Ishimae, M Seto, K Morishita, K Suzuki, R Ueda, K Ueda, N Kamada, M Greaves, GENES CHROMOSOMES & CANCER, 32, 3, 212, 221,   2001 11 , 10.1002/gcc.1185
    Summary:We report a novel MLL-associated chromosome translocation t(11;14)(q23;q24) in a child who showed signs of acute undifferentiated leukemia 3 years after intensive chemotherapy, that included the topoisomerase-II inhibitor VP 16. Screening of a cDNA library of the patient's leukemic cells showed a novel fusion transcript between MLL and the Gephyrin (GPHN) gene on 14q24. The resulting MLL-GPHN fusion gene encodes MLL AT hook motifs and a DNA methyltransferase homology domain fused to the C-terminal half of Gephyrin, including a presumed tubulin binding site and a domain homologous to the Escherichia coli molybdenum cofactor biosynthesis protein MoeA. Genomic breakpoint analysis showed potential, in vitro topoisomerase-II DNA-binding sites spanning the breakpoints in both MLL and GPHN but no flanking sequences that might mediate homologous recombination. This suggests that MLL-GPHN may have been generated by VP 16/topoisomerase-II-induced DNA double-strand breaks, followed by error-prone DNA repair via non-homologous end joining. Gephyrin was originally identified as a submembraneous scaffold protein that anchors and immobilizes postsynaptic membrane neurotransmitter receptors to underlying cytoskeletal elements. It also is reported to bind to phosphatidylinositol 3,4,5-triphosphate binding proteins involved in actin dynamics and downstream signaling and, interacts with ATM-related family member RAFTI. Gephyrin domains in the chimeric protein therefore could contribute novel signal sequences or might modify MLL activity by oligomerization or intracellular redistribution. (C) 2001 Wiley-Liss, Inc.
  • Regulatory network of mitomycin C action in human colon cancer cells, K Suzuki, W Yamamoto, JS Park, H Hanaoka, R Okamoto, Y Kirihara, T Yorishima, T Okamura, T Kumazaki, M Nishiyama, JAPANESE JOURNAL OF CANCER RESEARCH, 90, 5, 571, 577,   1999 05
    Summary:A network composed of activation and inactivation pathways to regulate mitomycin C (MMC) action is suggested to exist in human cancer cells. COLO201 colon cancer cells were stably transfected with human NQO1 cDNA that encodes NAD(P)H:quinone oxidoreductase (DT-diaphorase, DTD), and a clonal cell line with about 57-fold elevated DTD activity was obtained. Northern analysis revealed that expression of the NADPH:cytochrome P450 reductase (P450 reductase) gene was decreased in the transfectant, COLO201/NQO1, associated with the increase of NQO1 expression. Biochemical characterization of the cells showed a significant increase of the glutathione (GSH) content concomitantly with the decrease of the P450 reductase activity. As a result of these coordinated modulations, sensitivity of COLO201/NQO1 to MMC was not increased as compared to the parent cells. Analyses of inhibition by specific inhibitors of DTD, P450 reductase and glutathione S-transferase (GST) in 5 human colon cancer cell lines including the transfectant showed that DTD and P450 reductase play significant roles in MMC: activation in cells with sufficiently high DTD activity and with marginal DTD activity, respectively. In contrast, GST appeared to participate in MMC inactivation in cells with a high level of GST activity These results indicated that DTD, P450 reductase, GSH and GST may act together compensatively or competitively, depending on their levels in cells, to determine the cellular sensitivity to MMC.
  • Fusion of ETV6 to neurotrophin-3 receptor TRKC in acute myeloid leukemia with t(12;15)(p13;q25), M Eguchi, M Eguchi-Ishimae, A Tojo, K Morishita, K Suzuki, Y Sato, S Kudoh, K Tanaka, M Setoyama, F Nagamura, S Asano, N Kamada, BLOOD, 93, 4, 1355, 1363,   1999 02
    Summary:Chromosome translocations involving band 12p13 are known to be involved in a variety of hematologic malignancies, some of them resulting in rearrangement of the ETV6/TEL gene. Applying the fluorescence in situ hybridization (FISH) method, we found a cryptic translocation t(12;15)(p13;q25) in an adult acute myeloid leukemia (AML) patient. Hybridization with cosmid probes showed that the ETV6 gene was rearranged in this translocation. A patient-specific cDNA library was screened with ETV6 cDNA, and a novel fusion transcript was identified between the ETV6 and TRKC/NTRK3 gene located on 15q25. TRKC is a receptor tyrosine kinase that is activated by neurotrophin-3 (NT-3). It is known to be expressed broadly in neural tissues but not in hematologic cells, so far. ETV6-TRKC chimeric transcript encoded the pointed (PNT) domain of the ETV6 gene that fused to the protein-tyrosine kinase (PTK) domain of the TRKC gene. Two types of fusion transcript were determined, one that included the entire PTK domain of TRKC and the other in which the 3'-terminal 462 bp of TRKC was truncated within the PTK domain. Western blot analysis showed the expression of both chimeric proteins of 52 and 38 kD in size. Our results suggest that chimeric PTK expressed in the leukemic cells may contribute to cellular transformation by abnormally activating TRK signaling pathways. Moreover, this is the first report on truncated neurotrophin receptors associated in leukemia. (C) 1999 by The American Society of Hematology.
  • Cloning and nucleotide sequence of the gene encoding yeast ribosomal protein YS25. (jointly worked), Nucleic Acids Res., 16, 13, 6223,   1998 , 10.1093/nar/16.13.6223
  • Molecular targeting of mitomycin C chemotherapy, M Nishiyama, K Suzuki, T Kumazaki, W Yamamoto, T Toge, T Okamura, K Kurisu, INTERNATIONAL JOURNAL OF CANCER, 72, 4, 649, 656,   1997 08 , 10.1002/(SICI)1097-0215(19970807)72:4<649::AID-IJC17>3.0.CO;2-6
    Summary:In 10 human cancer cell lines, the activity of mitomycin C (MMC) was found to be determined by an interplay between activation by DT-diaphorase (DTD) and inactivation by glutathione S-transferase (GST). NADPH/cytochrome P-450 reductase was not responsible for MMC activation and expression of MDRI (Mr 170,000 P-glycoprotein), and MRP (multidrug resistance-associated protein) genes did not relate to MMC resistance. Gene expression analysis for NQOI (DTD gene) and GST ir predicted which enzyme activity predominated in a cell line, except K562 and K562/DOX. For tumors with DTD activity only, MMC given by itself was most active. In cell lines in which DTD action was predominant, tumor selectivity was achieved by enhancing DTD-mediated activation with m-iodobenzylguanidine and hyperglycemia, which reduced the intra-tumoral pH. KW2149, a novel MMC analogue activated by glutathione, was most active against tumors in which GST pi predominated. These various enzyme-specific effects could be observed even in cell lines derived from tumors with multidrug resistance. Such MMC treatment based on cell enzymology may enhance significantly MMC efficacy, helping to overcome multidrug resistance. (C) 1997 Wiley-Liss, Inc.
  • Molecular targeting chemotherapy for glioblastoma, Tatsunori Okamura, Masahiko Nishiyama, Katsuyuki Suzuki, Kaoru Kurisu, Wataru Yamamoto, Annals of Cancer Research and Therapy, 6, 1, 27, 31,   1997 , 10.4993/acrt1992.6.27
    Summary:We investigated the critical determinants of cytotoxic activity for cisplatin (CDDP), mitomycin C (MMC), and nimustine hydrochloride (ACNU), which are commonly used to treat malignant glioma. In 10 human cancer cell lines, glutathione S-transferase (GST) was a significant resistance factor for CDDP. MMC activity was found to be determined through the balance between activation by NADPH: quinone oxidoreductase (DTD) and inactivation by GST, while NADPH: cytochrome P450 reductase (P-450) was important in ACNU resistance. Two glioblastoma cell lines, T98G and U-251 MG, showed remarkably high levels of these 3 enzymes and glutathione (GSH), thus being moderately sensitive to MMC and resistant to CDDP and ACNU. Inhibition of these target enzymes caused an increase of the efficacy of each drug. KW2149, a novel MMC analogue activated by GSH, was active against T98G and U-251 MG cells due to their high GSH levels. Molecular targeting to seek the best treatment modality or the most active drug may contribute to improving the effectiveness of glioma chemotherapy. © 1997, The Japanese Society of Strategies for Cancer Research and Therapy. All rights reserved.
  • A new nomenclature for the cytoplasmic ribosomal proteins of --. (jointly worked), Nucleic Acids Res., 25, 24, 4872, 4875,   1997 , 10.1093/nar/25.24.4872
  • THE CARBOXYL EXTENSIONS OF 2 RAT UBIQUITIN FUSION PROTEINS ARE RIBOSOMAL-PROTEINS S27A AND L40, YL CHAN, K SUZUKI, IG WOOL, BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 215, 2, 682, 690,   1995 10 , 10.1006/bbrc.1995.2518
    Summary:Two rat recombinant cDNAs were characterized; they encode fusion proteins that have at their NH2 terminus the conserved 76 amino acid ubiquitin and at their carboxyl terminus the extension ribosomal proteins S27a (SO amino acids and a molecular weight of 9,397) or L40 (52 amino acids and a molecular weight of 6,177). The fusion proteins are processed in a reticulocyte lysate to ubiquitin and either S27a or L40. Hybridization of cDNAs to digests of nuclear DNA suggests that there are 14 to 19 copies of the S27a, and 6 to 10 of the L40, genes. The mRNA for ubiquitin-S27a has about 700 nucleotides and ubiquitin-L40 about 650. Ribosomal proteins S27a and L40 contain zinc finger motifs of the C-2-C-2 variety. S27a and L40 are related to ribosomal proteins from other species. (C) 1995 Academic Press, Inc.
  • GENOMIC ORGANIZATION AND ISOFORMS OF THE MOUSE ELP GENE, Y NINOMIYA, M OKADA, N KOTOMURA, K SUZUKI, T TSUKIYAMA, O NIWA, JOURNAL OF BIOCHEMISTRY, 118, 2, 380, 389,   1995 08
    Summary:Analysis was made on the genomic structure, functions, and expression of the mouse ELF gene, which codes for the embryonal long terminal repeat binding protein, Extensive screening of the cDNA library of embryonal carcinoma cells (EC cells) identified four isoforms of ELF: ELP1 (the original ELF isolate), ELP2, ELP3, and Ad4BP/SF1. Analysis of the genomic sequences revealed that these ELF isoforms were generated by alternative promoter usage and differential splicing. The mRNAs of isoforms initiated at four transcription start sites distributed on three exons, Sequence analysis of the four isoforms identified three polypeptides. The N-terminal portion of ELP1 and ELP2 was longer than ELP3, and Ad4BP/SF1 by 77 aa. The DNA-binding domain and region II were shared by all four isoforms. The C-terminal portion shared by ELP2, ELP3, and Ad4BP/SF1 was 131 aa in length, and that specific to ELP1 was 57 aa in length. The ELP3 and Ad4BP/SF1 isoforms were identical for the coding sequence, but the two differed at the 5' noncoding region, Region II and III domains of nuclear receptors mere thought to be involved in ligand-binding and transcriptional activation. ELP1, which lacked region III, functioned as a repressor, The isoforms carrying intact region II and region III functioned as transactivators. Expression of the four isoforms was studied in mouse tissues and in tissue culture cells by quantitative reverse transcriptase-polymerase chain reaction (RT-PCR) analysis. Complex patterns of expression of these isoforms were observed in various tissues. All four ELF isoforms were expressed only in EC cells.
  • CHARACTERIZATION BY MOLECULAR-CLONING OF 2 GENES FROM STREPTOMYCES-VERTICILLUS ENCODING RESISTANCE TO BLEOMYCIN, M SUGIYAMA, CJ THOMPSON, T KUMAGAI, K SUZUKI, R DEBLAERE, R VILLARROEL, J DAVIES, GENE, 151, 1-2, 11, 16,   1994 12 , 10.1016/0378-1119(94)90626-2
    Summary:Extracts of a bleomycin (Bm)-producing Streptomyces verticillus ATCC15003 were found to possess an acetyltransferase activity which inactivates Bm in the presence of acetyl coenzyme A. DNA fragments of S. verticillus were introduced into S. lividans by cloning and transformants selected for resistance to Bm. Deletion mapping and subcloning of a 6-kb DNA fragment showed the presence of two resistance determinants, blmA and blmB. The acetyltransferase activity was encoded by blmB; nucleotide sequence analysis identified an ORF consisting of 301 amino acids (aa) proposed to be that of Bm acetyltransferase (Bat). S. lividans and Escherichia coli transformants harboring plasmids carrying blmB produced an acetyltransferase which modified and determined resistance to Bm and structurally related antibiotics; this resistance gene has potential as a selective marker in gene transfer studies. Nucleotide sequence analysis of blmA revealed an ORF encoding 122 aa that had significant sequence similarity to the gene encoding the Bm-binding protein (Shble) identified by Gatignol et al. [FEBS Lett, 230 (1988) 171-175] in Streptoalloteichus hindustanus, the tallysomycin-producer. The blmA gene was expressed in E. coli and the resulting protein, like the Shble protein, prevents in vitro Bm-induced DNA breakage.
  • IDENTIFICATION OF ILLEGITIMATE RECOMBINATION HOT-SPOT OF THE RETINOIC ACID RECEPTOR-ALPHA GENE INVOLVED IN 15,17-CHROMOSOMAL TRANSLOCATION OF ACUTE PROMYELOCYTIC LEUKEMIA, S TASHIRO, N KOTOMURA, K TANAKA, K SUZUKI, T KYO, H DOHY, O NIWA, N KAMADA, ONCOGENE, 9, 7, 1939, 1945,   1994 07
    Summary:Acute promyelocytic leukemia (APL) has been characterized by 15;17 chromosomal translocation, which involves the retinoic acid receptor alpha (RARA) gene on chromosome 17 and the PML gene on chromosome 15. The breakpoints have been mapped to three cluster regions in the PML gene, and to RARA gene intron 2. We have examined the distribution of breakpoints within RARA gene intron 2. An extremely restricted region (ERR) of 50 bp within RARA gene intron 2 was identified as the duster region of breakpoints by polymerase chain reaction and sequence analysis of DNA from APL patients. To study experimentally the mechanism involved in the translocation, ERR was tested in NIH3T3 cells by in vitro transfection-recombination assay, in which target sequences were placed either downstream of the SV40 promoter or upstream of the neo gene. Cells were conferred resistance to G418 only when the promoter was fused to the neo gene by recombination of two target sequences during transfection. The molecular junctions were analysed in five clones, and all of them were shown to be confined within a 20 bp region in a 148 bp DNA fragment containing ERR. This suggests that ERR might be the illegitimate recombination hot spot in mammalian cells.
  • DETECTION OF PML RETINOIC ACID RECEPTOR-ALPHA GENE REARRANGEMENTS BY POLYMERASE CHAIN-REACTION USING GENOMIC DNA IN PATIENTS WITH ACUTE PROMYELOCYTIC LEUKEMIA, S TASHIRO, K TANAKA, H ASOU, T KYO, H DOHY, K SUZUKI, N KAMADA, JAPANESE JOURNAL OF CANCER RESEARCH, 84, 2, 110, 113,   1993 02
    Summary:Breakpoints of the 15;17 translocation in patients with acute promyelocytic leukemia (APL) have been identified within PML and retinoic acid receptor a (RARA) genes in chromosomes 15 and 17, respectively. A wide heterogeneity was observed in the breakpoints on the PML and RARA genes. Therefore, amplification of the breakpoints region by polymerase chain reaction (PCR) with DNA has been considered to be difficult. In the present study, a method was developed to detect the 15;17 translocation with genomic DNA. Of 13 patients with APL, four were detected to have the rearrangement of genomic DNA. At present, reverse transcriptase-polymerase chain reaction analysis is one of the methods available for diagnosis and detection of the residual leukemic cells in APL. In this study, PCR analysis using genomic DNA of APL cells is proved to be useful for identifying the breakpoints of the PML and the RARA genes. Furthermore, this method is applicable to patients for whom RNA samples of the leukemic cells are not available.
  • ZINC FINGER-LIKE MOTIFS IN RAT RIBOSOMAL-PROTEINS S27 AND S29, YL CHAN, K SUZUKI, J OLVERA, IG WOOL, NUCLEIC ACIDS RESEARCH, 21, 3, 649, 655,   1993 02 , 10.1093/nar/21.3.649
    Summary:The primary structures of the rat 40S ribosomal subunit proteins S27 and S29 were deduced from the sequences of nucleotides in recombinant cDNAs and confirmed by determination of amino acid sequences in the proteins. Ribosomal protein S27 has 83 amino acids and the molecular weight is 9,339. Hybridization of cDNA to digests of nuclear DNA suggests that there are 4 - 6 copies of the S27 gene; the mRNA for the protein is about 620 nucleotides in length. Ribosomal protein S29 has 55 amino acids and the molecular weight is 6,541. There are 14 - 17 copies of the S29 gene and its mRNA is about 500 nucleotides in length. Rat ribosomal protein S29 is related to several members of the archaebacterial and eubacterial S14 family of ribosomal proteins. S27 and S29 have zinc finger-like motifs as do other proteins from eukaryotic, archaebacterial, eubacterial, and mitochondrial ribosomes. Moreover, ribosomes and ribosomal subunits appear to contain zinc and iron as well.
  • THE PRIMARY STRUCTURE OF RAT RIBOSOMAL-PROTEIN L23A - THE APPLICATION OF HOMOLOGY SEARCH TO THE IDENTIFICATION OF GENES FOR MAMMALIAN AND YEAST RIBOSOMAL-PROTEINS AND A CORRELATION OF RAT AND YEAST RIBOSOMAL-PROTEINS, K SUZUKI, IG WOOL, JOURNAL OF BIOLOGICAL CHEMISTRY, 268, 4, 2755, 2761,   1993 02
    Summary:The amino acid sequence of the rat 60 S ribosomal subunit protein L23a was deduced from the sequence of nucleotides in a recombinant cDNA. Ribosomal protein L23a has 156 amino acids and a molecular weight of 17,684. Hybridization of the L23a cDNA to digests of nuclear DNA suggests that there are 18-20 copies of the L23a gene. The mRNA for the protein is about 600 nucleotides in length. Rat L23a is related to the yeast Saccharomyces cerevisiae L25, to the archaebacterial Methanococcus vannielii L23, to eubacterial Escherichia coli L23, and to other members of the L23 family of ribosomal proteins. A novel application of a routine homology search procedure was employed to identify a nucleotide sequence that could be used to design an oligodeoxynucleotide probe to screen a library for a cDNA that encodes rat L23a; this same procedure uncovered a number of previously unidentified genes for yeast ribosomal proteins in the Gen-Bank DNA data base. In a correlation of rat and yeast ribosomal proteins 48 pairs are shown to be related.
  • The ribosomal proteins : Major protein species are maintained throughout all organisms on the earth, according to evolutionary analyses. (jointly worked), Bol. Biol. (Life Sci. Adv. ), 12, 145, 163,   1993
  • The ribosomal Proteins : II. Alignments of the equivalents of ribosomal large subunit proteins from Escherichia coli, compiled by a universal code system. (jointly worked), Protein Sequences and Data Analysis, 5, 6, 301, 313,   1993
  • Yeast ribosomal proteins: XIV. Complete nucleotide sequences of the two genes encoding Saccharomyces cerevisiae YL16, Tetsuo Hashimoto, Katsuyuki Suzuki, Keiko Mizuta, Eiko Otaka, BBA - Gene Structure and Expression, 1132, 2, 195, 198,   1992 09 24 , 10.1016/0167-4781(92)90011-N
    Summary:We isolated and sequenced YL16A and YL16B encoding ribosomal protein YL16 of Saccharomyces cerevisiae. The two nucleotide sequences within coding regions retain 91.1% identity, and their predicted sequences of 176 amino acids show 93.8% identity. Out of the ribosomal protein sequences from various organisms currently available, no counterpart to YL16 could be found. © 1992.
  • PRIMARY STRUCTURE OF RAT RIBOSOMAL PROTEIN-S2 - A RIBOSOMAL-PROTEIN WITH ARGININE-GLYCINE TANDEM REPEATS AND RGGF MOTIFS THAT ARE ASSOCIATED WITH NUCLEOLAR LOCALIZATION AND BINDING TO RIBONUCLEIC-ACIDS, K SUZUKI, J OLVERA, IG WOOL, JOURNAL OF BIOLOGICAL CHEMISTRY, 266, 30, 20007, 20010,   1991 10
    Summary:The amino acid sequence of the rat 40 S ribosomal subunit protein S2 was deduced from the sequence of nucleotides in two recombinant cDNAs and confirmed from the amino acid sequence of a cyanogen bromide peptide obtained from the protein. Ribosomal protein S2 has 293 amino acids and has a molecular weight of 31,211. Hybridization of the cDNA to digests of nuclear DNA suggests that there are 23-28 copies of the S2 gene. The mRNA for the protein is about 1,000 nucleotides in length. The highly conserved repetitive mammalian gene family designated LLRep3, but not identified before, encodes ribosomal protein S2. Rat S2 is related to Saccharomyces cerevisiae S4, Methanococcus vannielii S5, Escherichia coli S5, and other members of the prokaryotic S5 family. S. cerevisiae S4 and E. coli S5 are involved in the binding of aminoacyl-tRNA to ribosomes and in conditioning the fidelity of translation; it is plausible to assume that rat S2 serves similar functions. The NH2-terminal region of S2 is rich in arginine-glycine repeats including eight that occur in tandem and has two consecutive copies of the motif RGGF; these sequences have been associated with nucleolar localization and binding to RNA.
  • THE PRIMARY STRUCTURE OF RAT RIBOSOMAL PROTEIN-L17, K SUZUKI, IG WOOL, BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 178, 1, 322, 328,   1991 07 , 10.1016/0006-291X(91)91817-V
  • THE PRIMARY STRUCTURE OF RAT RIBOSOMAL PROTEIN-P0, PROTEIN-P1, AND PROTEIN-P2 AND A PROPOSAL FOR A UNIFORM NOMENCLATURE FOR MAMMALIAN AND YEAST RIBOSOMAL-PROTEINS, IG WOOL, YL CHAN, A GLUCK, K SUZUKI, BIOCHIMIE, 73, 7-8, 861, 870,   1991 07 , 10.1016/0300-9084(91)90127-M
    Summary:The covalent structures of rat ribosomal proteins P0, P1, and P2 were deduced from the sequences of nucleotides in recombinant cDNAs. P0 contains 316 amino acids and has a molecular weight of 34 178; P1 has 114 residues and a molecular weight of 11 490: and P2 has 115 amino acids and a molecular weight of 11 684. The rat P-proteins have a near identical (16 of 17 residues) sequence of amino acids at their carboxyl termini and are related to analogous proteins in other eukaryotic species. A proposal is made for a uniform nomenclature for rat and yeast ribosomal proteins.
  • Yeast ribosomal proteins: XII. YS11 of Saccharomyces cerevisiae is a homologue to E.coli S4 according to the gene analysis, Keiko Mizuta, Tetsuo Hashimoto, Katsuyuki Suzuki, Eiko Otaka, Nucleic Acids Research, 19, 10, 2603, 2608,   1991 05 25 , 10.1093/nar/19.10.2603
    Summary:We isolated and sequenced a gene, YS11A, encoding ribosomal protein YS11 of Saccharomyces cerevisiae. YS11A is one of two functional copies of the YS11 gene, located on chromosome XVI and transcribed in a lower amount than the other copy which is located on chromosome II. The disruption of YS11A has no effect on the growth of yeast. The 5′-flanking region contains a similar sequence to consensus UASrpg and the T-rich region. The open reading frame is interrupted with an intron located near the 5′-end. The predicted amino acid sequence reveals that yeast YS11 is a homologue to E. coli S4, one of the ram proteins, three chloroplast S4s and others out of the ribosomal protein sequences currently available.
  • THE PRIMARY STRUCTURE OF RAT RIBOSOMAL PROTEIN-S7, K SUZUKI, J OLVERA, IG WOOL, FEBS LETTERS, 271, 1-2, 51, 53,   1990 10 , 10.1016/0014-5793(90)80369-T
  • THE PRIMARY STRUCTURE OF RAT RIBOSOMAL PROTEIN-L12, K SUZUKI, J OLVERA, IG WOOL, BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 172, 1, 35, 41,   1990 10 , 10.1016/S0006-291X(05)80169-X
  • THE PRIMARY STRUCTURE OF RAT RIBOSOMAL PROTEIN-S13, K SUZUKI, J OLVERA, IG WOOL, BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 171, 2, 519, 524,   1990 09 , 10.1016/0006-291X(90)91176-S
  • THE PRIMARY STRUCTURE OF RAT RIBOSOMAL PROTEIN-L9, K SUZUKI, J OLVERA, IG WOOL, GENE, 93, 2, 297, 300,   1990 09 , 10.1016/0378-1119(90)90239-N
  • THE PRIMARY STRUCTURE OF RAT RIBOSOMAL-PROTEIN S19, K SUZUKI, J OLVERA, IG WOOL, BIOCHIMIE, 72, 4, 299, 302,   1990 04 , 10.1016/0300-9084(90)90088-X
  • THE PRIMARY STRUCTURE OF RAT RIBOSOMAL PROTEIN-L35, K SUZUKI, J OLVERA, IG WOOL, BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 167, 3, 1377, 1382,   1990 03 , 10.1016/0006-291X(90)90675-D
  • Yeast ribosomal proteins: XI. Molecular analysis of two genes encoding YL41, an extremely small and basic ribosomal protein, from Saccharomyces cerevisiae, Katsuyuki Suzuki, Tetsuo Hashimoto, Eiko Otaka, Current Genetics, 17, 3, 185, 190,   1990 03 , 10.1007/BF00312608
    Summary:Two genes encoding ribosomal protein YL41 were cloned from Saccharomyces cerevisiae chromosomal DNA. Both genes contain an uniterrupted region of only 75 nucleotides coding for a protein of 3.3 kD. Within the coding regions the nucleotide sequences are virtually identical, whereas in both the 5′-and 3′-flanking regions the two genes differ significantly from each other. The deduced protein shows an arginine and lysine content of 68 percent, i.e., 17 out of 25 residues, and the basic residues are evenly distributed over the molecule. When compared to the ribosomal protein sequences currently available no counterpart to YL41 could be found in prokaryotes and it seems likely that YL41 is a eukaryotespecific ribosomal protein. © 1990 Springer-Verlag.
  • Examination of protein sequence homologies VII. The complementary molecular coevolution of ribosomal proteins equivalent to - -L7/L12 and L10. (jointly worked), Protein Seq. Data Anal., 3, 1, 11, 19,   1990
  • Structural comparison of 26S rRNA-binding ribosomal protein L25 from two different yeast strains and the equivalent proteins from three eubacteria and two chloroplasts, H. A. Raué, E. Otaka, K. Suzuki, Journal of Molecular Evolution, 28, 5, 418, 426,   1989 05 , 10.1007/BF02603077
    Summary:The sequences of Saccharomyces carlsbergensis ribosomal protein (r-protein) SL25* and its equivalents from Candida utilis (CL25), Escherichia coli (EL23), Bacillus stearothermophilus (BL23), Mycoplasma capricolum (ML23), Marchantia polymorpha chloroplasts (McpL23), and Nicotiana tabacum chloroplasts (NcpL23) were examined using a computer program that evaluates the extent of sequence similarity by calculating correlation coefficients for each pair of residues in two proteins from a number of physical properties of individual amino acids. Comparison matrices demonstrate that the prokaryotic sequences (including McpL23 and NcpL23) can be aligned unambiguously by introducing small internal deletions/insertions at three specific positions. A similar comparison brought to light a clear evolutionary relationship between the prokaryotic and the yeast proteins despite the fact that visual inspection of these sequences revealed only limited similarity. The alignment deduced from this comparison shows the two yeast r-proteins to have acquired a long (50-60 amino acids) N-terminal extension as well as a 13-amino acid-long deletion near the C-terminus. The significance of these findings in terms of the evolution of r-proteins in general and the biological function of various parts of the SL25 protein in particular is discussed. © 1989 Springer-Verlag New York Inc.
  • Examination of protein sequence homologies VI. The evolution of - -L7/L12 equivalent ribosomal proteins('A' proteins), and the tertiary structure. (jointly worked), Protein Seq. Data Anal., 2, 5, 395, 402,   1989
  • Proteolytic Processing of Glucoamylase in the Yeast Saccharomyces diastaticus, Ichiro Yamashita, Katsuyuki Suzuki, Sakuzo Fukui, Agricultural and Biological Chemistry, 50, 2, 475, 482,   1986 , 10.1271/bbb1961.50.475
    Summary:Glucoamylase was purified from the culture fluid of the yeast Saccharomyces diastaticus carrying STA1. The molecular weight of the protein was about 250K by both gel. Filtration and acrylamide gel electrophoresis. The protein was glycosylated with asparagine-linked glycosides whose molecular weight was 70 K. The amino-terminal sequence of the protein began from the 33rd amino acid residue from the first methionine of the putative precursor deduced from the DNA sequence of STA1. The amino acid composition of the purified protein matched the predicted amino acid composition. These results confirmed that STA1 codes for a structural gene of glucoamylase. Yeast cells secreted enzymatically active β-lactamase into the culture medium after transformation with hybrid plasmids containing the glucoamylase promoter and the DNA sequence encoding the extended peptide of 32 amino acids fused to a structural gene for Escherichia coli β-lactamase. The result suggested that the amino-terminal peptide of the putative glucoamylase precursor functions as a signal sequence for protein secretion. Taking into consideration the subunit structure of the previously purified glucoamylase [Yamashita et al., Agric. Biol. Chem. 48, 1611 (1984)], we present the molecular structure of the glucoamylase precursor and also a model for its proteolytic processing. © 1986, Japan Society for Bioscience, Biotechnology, and Agrochemistry. All rights reserved.
  • Gene products specifically changed during the sexual response of --. (jointly worked), Katsuyuki SUZUKI, Eiko TSUCHIYA, Tokichi MIYAKAWA, Sakuzo FUKUI, Agric. Biol. Chem., 49, 8, 2471, 2473,   1985 , 10.1271/bbb1961.49.2471
  • NUCLEOTIDE-SEQUENCE OF THE EXTRACELLULAR GLUCOAMYLASE GENE STA1 IN THE YEAST SACCHAROMYCES-DIASTATICUS, YAMASHITA, I, K SUZUKI, S FUKUI, JOURNAL OF BACTERIOLOGY, 161, 2, 567, 573,   1985
  • In vivo ligation of linear DNA molecules to circular froms in the yeast --.(jointly worked), J. Bacteriol., 155, 2, 747, 754,   1983
  • HIGH-FREQUENCY TRANSFORMATION OF SACCHAROMYCES-CEREVISIAE WITH LINEAR DEOXYRIBONUCLEIC-ACID, Y IMAI, K SUZUKI, YAMASHITA, I, S FUKUI, AGRICULTURAL AND BIOLOGICAL CHEMISTRY, 47, 4, 915, 918,   1983 , 10.1271/bbb1961.47.915

Research Grants & Projects

  • Molecular evolution of Nitrogen-fixation genes
  • Evolutionary Engineering of Biopolymer
  • Study on Structure-function Relationship of Eukaryotic Ribosomal Proteins