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橋本昌征 Masayuki Hashimoto

 

 

Masayuki Hashimoto

橋本昌征 助理教授 (Masayuki Hashimoto)

E-mail:hashmate@mail.ncku.edu.tw

TEL:06-2353535 ext 3615/3621

FAX:06-2095845

 

Educations / Employment Experience

 

Educations 2000/ 03 Ph. D. (Dr. of Agriculture) from Graduate School of Science and Technology, Niigata University (Niigata, Japan).
  1996/ 03 Master's degree from Graduate School of Agriculture, Niigata University (Niigata, Japan).
  1994/ 03 Graduated from Department of Agricultural Chemistry, Niigata University (Niigata, Japan).
   

 

Employment history

2019/ 02 - Now

Assistant Professor, Institute of Molecular Medicine, National ChengKung University Medical College, Tainan, Taiwan

 

2013/ 05 - 2019/01

Project Assistant Professor, Institute of Molecular Medicine, National ChengKung University Medical College, Tainan, Taiwan

 

2007/ 11 - 2013/ 04

Assistant Professor, Young Researchers Empowerment Center, Shinshu Uni

 

2005/ 06 - 2007/ 10

Assistant Professor, Division of Gene Research Center, Human and Environment Science Research Center, Shinshu University.

 

2002/ 08 - 2005/ 05

Postdoctoral research fellow of Department of Biology, Tokyo Metropolitan University.

 

2002/ 04 - 2002/ 07

Postdoctoral research fellow of Kyowa Hakko Co., Ltd., detached to Department of Biology, Tokyo Metropolitan University.

 

2000/ 04 - 2002/ 03

Postdoctoral research fellow of Bio-oriented Technology Research Advancement Institution, detached to Department of Agricultural Chemistry, Shizuoka University.

 

Research goal

 

I plan to design and build a bacterial genome eventually. This is also a big goal for synthetic biology. But the benefits of the achievement will be incredible. It will enable to create specific bacteria to solve various problems in health, energy, materials, food and so on. For the aim, understand whole life mechanism in a cell is necessary. A well studied and simple organism will take us to the goal faster. Therefore, I have studied bacterial physiology and genomic engineering in some model bacteria.

   

Current interests

 

1) We develop a in vivo cloning method for long fragment which is too long for PCR amplification. We demonstrated to clone 40 and 80 kb fragment from gram negative bacteria. Then, we are going to expand the method in variety of bacteria and further long fragment.

2) We found that restriction-modification enzymes are involved in genomic evolution in uropathogenic E. coli. In addition, we identified several novel restriction enzymes. Then, we are going to characterize the novel enzymes and investigating the association between the gene and genomic evolution in pathogenic E. coli.

3) In some pathogenic bacteria like E. coli o157, the expression of toxin is triggered by prophage induction. Then, we are screening an inhibitor for the prophage induction to repress the toxin expression.

 

 

研究成果 Publications -- Masayuki Hashimoto

[Journal Articles]

  1. Kurata T, Nakanishi S, Hashimoto M, Taoka M, Isobe T, Kato JI. (2018) Subunit composition of ribosome in the yqgF mutant deficient in pre-16S rRNA processing of Escherichia coli. Journal of Molecular Microbiology and Biotechnology. 28(4):179-182.
  2. Suparthana IP, Duniaji AS, Hashimoto M. (2018) Investigation to Traditionally Produced Soybean Fermented Food (Sere kedele) in Gianyar region-Bali and Molecular Identification of Bacteria Involved in their Spontaneous Fermentation. Scientific Journal of Food Technology. 5 (2) 65-68
  3. Ueda D, Matsugane S, Okamoto W, Hashimoto M, Sato T. (2018) Non-enzymatic pathway with superoxide in intracellular terpenoid synthesis. Angew Chem Int Ed Engl. 57 (32) 10347-10351
  4. Yamada T, Miyashita M, Kasahara J, Tanaka T, Hashimoto M and Yamamoto H. (2018) The transmembrane segment of TagH is required for wall teichoic acid transport under heat stress in Bacillus subtilis. Microbiol. 164 (7) 935-945
  5. Hashimoto M, Matsushima H, Suparthana PI, Ogasawara H, Yamamoto H, Teng CH and Sekiguchi J. (2018) Digestion of peptidoglycan near the cross-link is necessary for the growth of Bacillus subtilis. Microbiol. 164 (3) 299-307
  6. Ho YC, Hung FR, Weng CH, Li WT, Chuang TH, Liu TL, Lin CY, Lo CJ, Chen CL, Chen JW, Hashimoto M, Hor LI. (2017) Lrp, a global regulator, regulates the virulence of Vibrio vulnificus. J Biomed Sci. 24 (1) 54.
  7. Pedrolli, D., Langer, S., Hobl, B., Schwarz, J., Hashimoto, M., Mack, M. (2015) The ribB FMN riboswitch from Escherichia coli operates at the transcriptional and translational level and regulates riboflavin biosynthesis. FEBS Journal. 282(16) 3230-42
  8. Kurata, T., Nakanishi, S., Hashimoto, M., Taoka, M., Yamazaki, Y., Isobe, T., and Kato, J. (2015) Novel essential gene involved in 16S rRNA processing in Escherichia coli. Journal of Molecular Biology. 427 (4) 955-965.
  9. Kiriyama, Y., Yazawa, K., Tanaka, T., Yoshikawa, R., Yamane, H., Hashimoto, M., Sekiguchi, J., and Yamamoto, H. (2014) Localisation and expression of the Bacillus subtilis DL-endopeptidase LytF are influenced by mutations in LTA synthases and glycolipid anchor synthetic enzymes. Microbiology. 160 (12) 2639-49.
  10. Hashimoto, M., Fujikura, K., Miyake, Y., Higashitsuji, Y., Kiriyama, Y., Tanaka, T, Yamamoto, H. and Sekiguchi, J. (2014) A cell wall protein (YqgA) is genetically related to the cell wall-degrading DL-endopeptidases in Bacillus subtilis. Biosci. Biotechnol. Biochem. 78 (8) 1428-34
  11. Chen, Y.W., Teng, C.H., Ho, Y.H., Jessica Ho, T.Y., Huang, W.C., Hashimoto, M., Chiang, I.Y. and Chen, C.S. (2014) Identification of bacterial factors involved in type 1 fimbria expression using an Escherichia coli K12 proteome chip. Mol. Cell Proteomics. 13: 1485-94.
  12. Hashimoto, C., Hashimoto, M., Honda, H., Kato, JI. (2013) Effects on IS1 transposition frequency of a mutation in the ygjD gene involved in an essential tRNA modification in Escherichia coli. FEMS Microbiol Lett. 347: 140–148.
  13. Langer, S., Hashimoto, M., Hobl, B., Mathes, T., Mack, M. (2013) Flavoproteins are potential targets for the antibiotic roseoflavin in Escherichia coli. J. Bacteriol. 195: 4037-4045.
  14. Hashimoto, M., Ooiwa, S. and Sekiguchi, J. (2012) The synthetic lethality of lytE cwlO in Bacillus subtilis is caused by lack of d, l-endopeptidase activity at the lateral cell wall. J. Bacteriol. 194: 796-803.
  15. Iwadate, Y., Honda, H., Sato, H., Hashimoto, M. and Kato J. (2011) Oxidative stress sensitivity of engineered Escherichia coli cells with a reduced genome. FEMS Microbiol Lett. 322: 25-33.
  16. 橋本昌征,山本博規,関口順一 (2009) 枯草菌における細胞の分離.繊維学会誌65: 282-286.
  17. Hashimoto, M. (2008) Genome engineering of Lactococcus lactis. Rep. Noda Inst. Sci. Res 52: 49-50.
  18. Yamamoto, H*., Hashimoto, M*., Higashitsuji, Y., Harada, H., Hariyama, N., Takahashi, L., Iwashita, T., Ooiwa, S. and Sekiguchi, J. (2008) Post-translational control of vegetative cell separation enzymes through a direct interaction with specific inhibitor IseA in Bacillus subtilis. Mol Microbiol. 70: 168-182. *: These authors are contributed equally to this work.
  19. Kato, J. and Hashimoto, M. (2008) Construction of long chromosomal deletion mutants of Escherichia coli and minimization of the genome. Methods Mol. Biol. 416:279-293.
  20. Kato, J., and Hashimoto, M. (2007) Construction of consecutive deletions of the Escherichia coli chromosome. Mol. Syst. Biol. 3: 132.
  21. Hashimoto, M., Mizutani, A., Tago, K., Ohnishi-Kameyama, M., Shimojo, T. and Hayatsu, M. (2006) Cloning and nulceotide sequence of carbaryl hydrolase gene (cahA) from Arthrobacter sp. RC100. J. Biosci. Bioeng. 101: 410-414.
  22. Tago, K., Yonezawa, S., Ohkouchi, T., Ninomiya, T., Hashimoto, M., Hayatsu, M. (2006) A novel organophosphorus pesticide hydrolase gene encoded on a plasmid in Burkholderia sp. strain NF100. Microbes. Environ. 21: 53-57.
  23. Tago, K., Yonezawa, S., Ohkouchi, T., Hashimoto, M., Hayatsu, M. (2006) Purification and characterization of fenitrothion hydrolase from Burkholderia sp. NF100. J. Biosci. Bioeng. 101: 80-82.
  24. Ote, T., Hashimoto, M., Ikeuchi, Y., Su'etsugu, M., Suzuki, T., Katayama, T. and Kato, J. (2005) Involvement of the Escherichia coli folate-binding protein YgfZ in RNA modification and regulation of chromosomal replication initiation. Mol. Microbiol. 59: 265-275.
  25. Hashimoto, M., Ichimura, T., Mizoguchi, H., Tanaka, K., Fujimitsu, K., Keyamura, K., Ote, T., Yamakawa, T., Yamazaki, Y., Mori, H., Katayama, T., and Kato, J. (2005) Cell size and nucleoid organization of engineered Escherichia coli cells with a reduced genome. Mol. Microbiol. 55: 137-149.
  26. Watanabe, T., Ariga Y., Sato, U., Toratani, T., Hashimoto, M., Nikaidou, N., Kezuka, Y., Nonaka, T. and Sugiyama, J. (2003) Aromatic residues within the substrate-binding cleft of Bacillus circulans chitinase A1 are essential for crystalline chitin hydrolysis. Biochem. J. 376: 237-244.
  27. Hashimoto, M. and Kato, J. (2003) Indispensability of the Escherichia coli carbonic anhydrases YadF and CynT in cell proliferation at a low CO2 partial pressure. Biosci. Biotech. Biochem. 67: 919-922.
  28. Hashimoto, M., Fukui, M., Hayano, K., and Hayatsu, M. (2002) Nucleotide sequence and genetic structure of a novel carbaryl hydrolase gene (cehA) from Rhizobium sp. AC100. Appl. Environ, Microbiol. 68: 1220-1227.
  29. Sasaki, C., Yokoyama, A., Itoh, Y., Hashimoto, M., Watanabe, T. and Fukamizo T. (2002) Comparative enzymology of family 18 chitinases from plants and microbes. J Biochem (Tokyo). 131:557-564.
  30. Jee, J.G., Ikegami, T., Hashimoto, M., Kawabata, T., Ikeguchi, M., Watanabe, T., and Shirakawa, M. (2002) Solution structure of the fibronectin type III domain from Bacillus circulans WL-12 Chitinase A1. J. Biol. Chem. 277: 1388-1397.
  31. Hayatsu, M., Mizutani, A., Hashimoto, M., Sato, K. and Hayano, K. (2001) Purification and characterization of carbaryl hydrolase from Arthrobacter sp. RC100. FEMS Microbiol Lett. 201: 99-103.
  32. Watanabe, T., Ishibashi, A., Ariga, Y., Hashimoto, M. , Nikaidou, N., Sugiyama, J., Matsumoto, T., and Nonaka, T. (2001) Trp122 and Trp134 on the surface of the catalytic domain are essential for crystalline chitin hydrolysis by Bacillus circulans chitinase A1. FEBS Lett. 494: 74-78.
  33. Honda, Y., Tanimori, S., Kirihata, M., Kaneko, S., Tokuyasu, K., Hashimoto, M., Watanabe, T., and Fukamizo, T. (2000) Kinetic analysis of the reaction catalyzed by chitinase A1 from Bacillus circulans WL-12 toward the novel substrates, partially N-deacetylated 4-methylumbelliferyl chitobiosides. FEBS Lett. 476: 194-197.
  34. Honda, Y., Tanimori, S., Kirihata, M., Kaneko, S., Tokuyasu, K., Hashimoto, M. and Watanabe, T. (2000) Chemo- and enzymatic synthesis of partially and fully N-deacetylated 4-methylumbelliferyl chitobiosides: fluorogenic substrates for chitinase. Bioorg Med Chem Lett. 10: 827-829.
  35. Hashimoto, M., Ikegami, T., Seino, S., Ohuchi, N., Fukada, H., Sugiyama, J., Shirakawa, M., and Watanabe, T. (2000) Expression and characterization of the chitin-binding domain of chitinase A1 from Bacillus circulans WL-12. J. Bacteriol. 182: 3045-3054.
  36. Ikegami, T., Okada, T., Hashimoto, M., Seino, S., Watanabe, T., and Shirakawa, M. (2000) Solution structure of the chitin-binding domain of Bacillus circulans WL-12 chitinase A1. J. Biol. Chem. 275: 13654-13661.
  37. 橋本昌征 、志田景子、渡邉剛志 (2000) フィブロネクチン・タイプIII様ドメインの大量発現系の構築とキチンとの相互作用. キチンキトサン研究 6: 1-8.
  38. Hashimoto, M., Honda, Y., Fukamizo, T., and Watanabe, T. (2000) Site-directed mutagenesis of Asp280 suggested substrate-assisted catalysis of chitinase A1 from Bacillus circulans WL-12. J. Biosci. Bioeng. 89: 100-102.
  39. Matsumoto, T., Nonaka, T., Hashimoto, M., Watanabe, T. , and Mitsui, Y. (1999) Three-dimensional structure of the catalytic domain of chitinase A1 from Bacillus circulans WL-12 at a very high resolution. Proc. Japan Acad. 75B: 269-274.
  40. Matsumoto, T., Nonaka, T., Katouda, H., Hashimoto, M., Watanabe, T. and Mitsui, Y. (1999) Crystallizaion and a preliminary crystallographic analysis of the catalytic domain of chitinase A1 from Bacillus circulans WL-12. Protein. Peptid. Lett. 6: 399-402.
  41. Sugiyama, J., Boisset, C., Hashimoto, M., and Watanabe, T. (1999) Molecular directionality of beta-chitin biosynthesis. J. Mol. Biol. 286: 247-255.
  42. Watanabe, T., Ito, Y., Yamada, T., Hashimoto, M., Sekine, S., and Tanaka, H. (1994) The roles of the C-terminal domain and type III domains of chitinase A1 from Bacillus circulans WL-12 in chitin degradation. J. Bacteriol. 176: 4465-4472.
  43. Sekine, S., Ito, Y., Hashimoto, M., Tanaka, H. and Watanabe, T. (1994) Characterization of monoclonal antibodies to chitinase A1 and enhancement of chitinase A1 activity by monoclonal antibodies. Biochem. Biophys. Res. Commun. 204: 7-16.

[Doctor thesis]

  1. 「細菌キチナーゼを構成するドメインの構造と機能」"Domain structure and function comprising bacterial chitinase" (2000) Graduate School of Science and Technology, Niigata University.

[Books]

  • 加藤潤一、橋本昌征 (2004) 「ゲノミクス・プロテオミクスの新展開」今中忠行監修、エヌ・ティー・エス出版、微生物の最小必須遺伝子群、22-30.

 

[Proceedings]

  1. Hashimoto, M., Matsushima, H., Sparthana, I.P., Ogasawara, H. and Sekiguchi, J. (2013) Function of essential peptidoglycan degrading enzymes localizing at cellular sidewall in Bacillus subtilis. 7th International conference on Gram-positive microorganisms.
  2. Hashimoto, M., Ooiwa, S., and Sekiguchi, J. (2011) Function of D,L- endopeptidases LytE and CwlO for cell elongation in Bacillus subtilis. 6th International conference on Gram-positive microorganisms.
  3. Hashimoto, M., Katoda, H., Seino, S., Matsumoto, T. , Nonaka, T. , Mitsui, Y., and Watanabe, T. (1999) Structure and function of the domains composing chitinase A1 of Bacillus circulans WL-12. Proceedings of MIE BIOFORUM 98. 644-653.
 

 

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