Life Science and Technology News

Labs spotlight #34 - Nakamura and Yatsunami Laboratory -

Extremophiles have limitless possibilities!

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March 9, 2017

The Department has a variety of laboratories for Life Science and Technology, in which cutting-edge innovative research is being undertaken not only in basic science and engineering but also in the areas of medicine, pharmacy, agriculture, and multidisciplinary sciences.

This "Spotlight" series features a laboratory from the Department and introduces you to the laboratory's research projects and outcomes. This time we focus on Nakamura and Yatsunami Laboratory.

Professor Satoshi Nakamura and Associate Professor Rie Yatsunami

Life Science and Technology
Professor Satoshi Nakamuraouter and Associate Professor Rie Yatsunamiouter

Degree Professor Satoshi Nakamura : PhD 1989, Tokyo Institute of Technology
Associate Professor Rie Yatsunami : PhD 2000, Tokyo Institute of Technology
Areas of Research Genetic engineering, Protein engineering, Directed evolution, Metabolic engineering
Keywords Extremophiles, Extremozymes, Alkaliphiles, Halophiles, Thermophiles, Carotenoid biosynthtesis, Glycogen biosynthtesis
Website Nakamura and Yatsunami Laboratory (Japanese)outer

Research interest

We are interested in extremozymes and functional proteins produced by extremophiles, such as alkaliphiles, halophiles, thermophiles, using genetic engineering, protein engineering and directed evolution.

Extremozymes and functional proteins include xylanase, chitinase, chitosanase, beta-1,3-glucanase, alpha-amylase, glucoamylase, 3-isopropylmalate dehydrogenase, arabinofuranosidase, ferredoxin, transducer, FtsZ, cruxrhodopsin, cruxhalorhodopsin, etc.

AFM image of a triangular disk-shaped extremely halophilic archaeon

AFM image of a triangular disk-shaped extremely halophilic archaeon

Research findings

Selected publications

Satoshi Nakamura

  • [1] Yang, Y., Yatsunami, R., Ando, A., Miyoko, N., Fukui, Takaichi, S., Nakamura, S. Complete biosynthetic pathway of the C50 carotenoid bacterioruberin from lycopene in the extremely halophilic archaeon Haloarcula japonica. J. Bacteriol., 197, 1614-1623 (2015).
  • [2] Yatsunami, R., Ando, A., Yang, Y., Takaichi, S., Kohno, M., Matsumura, Y., Ikeda, H., Fukui, T., Nakasone, K., Fujita, N., Sekine, M., T. Takashina, T., Nakamura, S. Identification of carotenoids from the extremely halophilic archaeon Haloarcula japonica. Front. Microbiol., 5, Article 100 (2014).
  • [3] Onodera, M., Yatsunami, R., Tsukimura, W., Fukui, T., Nakasone, K., Takashina, T., Nakamura, S. Gene analysis, expression, and characterization of an intracellular a-amylase from the extremely halophilic archaeon Haloarcula japonica. Biosci. Biotechnol. Biochem. 77, 281-288 (2013)
  • [4] Uni, F., Lee, S., Yatsunami, R., Fukui, T., Nakamura, S. Mutational analysis of a CBM family 5 chitin-binding domain of an alkaline chitinase from Bacillus sp. J813. Biosci. Biotechnol. Biochem. 76, 530-535 (2012)
  • [5] Yazawa, R., Takakura, J., Sakata, T., Ihsanawati, Yatsunami, R., Fukui, T., Kumasaka, T., Tanaka N., Nakamura, S. A calcium-dependent xylan-binding domain of alkaline xylanase from alkaliphilic Bacillus sp. strain 41M-1. Biosci. Bitechnol. Biochem. 75, 379-381 (2011)
  • [6] Tsukimura, W., Watanabe, K., Morokuma, C., Yatsunami, R., Fukui T., Nakamura, S. Improvement of alkaliphily of thermostable GH family 10 xylanase from Thermotoga maritima by directed evolution, J. Jpn. Soc. Extr. 9, 15-18 (2010)

Rie Yatsunami

  • [1] Endo, K., Nagao, K., Toyama, K., Ishida, S., Fukazawa, T., Yatsunami, R., Fukui, T., Xing, X., Nakamura, S. Cloning of a chitinase gene from newly isolated alkaliphilic Nocardiopsis sp. strain F96 and extracellular production of the recombinant protein in Escherichia coli. J. Jpn. Soc. Extremophiles, 14, 21-29 (2015).
  • [2] Yang, Y., Yatsunami, R., Ando, A., Miyoko, N., Fukui, T., Takaichi, S. Nakamura, S. Complete Biosynthetic Pathway of the C50 Carotenoid Bacterioruberin from Lycopene in the Extremely Halophilic Archaeon Haloarcula japonica. J. Bacteriol., 197, 1614-1623 (2015).
  • [3] Yatsunami, R., Ando, A., Yang, Y., Takaichi, S., Kohno, M., Matsumura, Y., Ikeda, H., Fukui, T., Nakasone, K., Fujita, N., Sekine, M., Takashina, T., Nakamura S. Identification of carotenoids from the extremely halophilic archaeon Haloarcula japonica. Front. Microbiol., 5, 100-105 (2014).
  • [4] Tadikara, T., Matsubara, T., Kubota, Y., Kosaka, T., Ozawa, T., Tsukimura, W., Yatsunami, R., Fukui, T., Nakasone, K., Takashina, T., Nakamura, S. Gene expression and characterization of aerotaxis transducer HemAT from extremely halohilic archaeon Haloarcula japonica TR-1. J. Jpn. Soc. Extremophiles. 12, 29-32 (2013).
  • [5] Onodera, M., Yatsunami, R., Tsukimura, W., Fukui, T., Nakasone, K., Takashina, T., Nakamura, S. Gene analysis, expression and characterization of an intracellular α-amylase from extremely halophilic archaeon Haloarcula japonica. Biosci. Biotechnol. Biochem., 77, 281-288 (2013).
  • [6] Uni, F., Lee, S., Yatsuanmi, R., Fukui, T., Nakamura, S. Mutational Analysis of a CBM Family 5 Chitin-Binding Domain of an Alkaline Chitinase from Bacillus sp. J813. Biosci. Biotechnol. Biochem., 76, 530-535 (2012).
  • [7] Chen, S., Ye, F., Chen Y., Zhao, H., Yatsunami, R., Nakamura, S., Arisaka, F., Xing, X.-H. Mechanism of the thermal inactivation of a MBP-fused heparinase I: Biochemical investigation and kinetic modeling. Biotechnol. Bioeng., 108, 1841-1851 (2011).
  • [8] Yazawa, R., Takakura J., Sakata, T., Ihsanawati, Yatsunami, R., Fukui, T., Kumasaka,T., Tanaka, N. Nakamura, S. A Calcium-Dependent Xylan- Binding Domain of Alkaline Xylanase from Alkaliphilic Bacillus sp. Strain 41M-1. Biosci. Biotechnol. Biochem., 75, 379-381(2011).

Contact

Professor Satoshi Nakamura
Room 907, J2-J3 building, Suzukakedai campus
E-mail : nakamura.s.af@m.titech.ac.jp

Associate Professor Rie Yatsunami
Room 908, J2-J3 building, Suzukakedai campus
E-mail : yatsunami.r.aa@m.titech.ac.jp

*Find more about the lab and the latest activities at the lab site (Japanese)outer.

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