Molecular and Chemical Life Science :
Chemical Biology


Professor TANAKA Yoshikazu
Campus Katahira campus
Laboratory Applied Biological Molecular Science
Tel +81-22-217-6205
E-mail yoshikazu.tanaka.e8@tohoku.ac.jp
Website http://www.lifesci.tohoku.ac.jp/labmos/index.html
 High resolution structure give us a lot of information important for understanding molecular mechanism. I use X-ray crystallography to study proteins that play important roles in biology and disease. Our laboratory started since 2017. We are always looking for motivated students who are interested in our research.
Mar. 1999                       Graduated from School of Engineering, Tohoku University
Mar. 2001                       Completed Master course, Graduate School of Engineering, Tohoku Univeristy
Mar. 2004                       Completed Ph.D. course, Graduate School of Engineering, Tohoku University
Apr. 2004 – Mar. 2006  Postdoctoral Researcher, Graduate School of Science, Hokkaido University
Apr. 2006 – Jan. 2008    Postdoctoral Researcher, Graduate School of Frontier Sciences, The University of Tokyo
Jan. 2008 – Mar. 2012   Tenure Track Assistant Professor, Creative Research Institution, Hokkaido University
Apr. 2010 - Mar.2017    Associate Professor, Faculty of Advanced Life Science, Hokkaido University
Oct. 2015-                        JST—PREST Researcher
Jul. 2016 – Mar. 2017     Guest Scientist, Max Planck Institute of Molecular Physiology
2017-                                Current position
Selected Publications
  1. Chen, M., Asai, S., Narai, S., Nambu, S., Omura, N., Sakaguchi, Y., Suzuki, T., Ikeda-Saito, M., Watanabe, K., Yao, M., Shigi, N., and, Tanaka, Y., Biochemical and structural characterization of oxygen-sensitive 2-thiouridine synthesis catalyzed by the iron-sulfur protein TtuA. Proc. Natl. Acad. Sci. USA, 114, 4954-4959 (2017)
  2. Gai, Z., Matsuno, A., Kato, K., Kato, S.,Khan, R.I., Shimizu, T., Yoshioka, T., Kato, Y., Kishimura, H., Kanno, G., Miyabe, Y., Terada, T., Tanaka, Y., and Yao, M., Crystal structure of the 3.8 MDa respiratory supermolecule hemocyanin at 3.0 angstrom resolution. Structure, 23, 2204-2212 (2015)
  3. Yamashita, D., Sugawara, T., Takeshita, M., Kaneko, J., Kamio, Y., Tanaka, I., Tanaka, Y., and Yao, M., Molecular basis of transmembrane beta-barrel formation of staphylococcal pore-forming toxins. Nature Commun., 5, 4897 (2014)
  4. Yu, F., Tanaka, Y., Yamashita, K., Suzuki, T., Nakamura, A., Hirano, N., Suzuki, T., Yao, M., and Tanaka, I., Molecular basis of dihydrouridine formation on tRNA. Proc. Natl. Acad. Sci. USA, 108, 19593-19598 (2011)
  5. Yamashita, K., Kawai, Y., Tanaka, Y., Hirano, N., Kaneko, J., Tomita, N., Ohta, M., Kamio, Y., Yao, M., and Tanaka, I., Crystal Structure of the Octameric Pore of Staphylococcal γ-hemolysin Reveals the β-barrel Pore Formation Mechanism by Two Components. Proc. Natl. Acad. Sci. USA, 108, 17314-17319 (2011)
  6. Tanaka, Y., Yamagata, S., Kitago, Y., Yamada, Y., Chimnaronk, S., Yao, M., and Tanaka, I., Deduced RNA binding mechanism of ThiI based on structural and binding analyses of a minimal RNA ligand, RNA, 15, 1498-1506 (2009)
  7. Tanaka, Y., Sakamoto, S., Kuroda, M., Goda, S., Gao, Y.-G., Tsumoto, K., Hiragi, Y., Yao, M., Watanabe, N., Ohta, T., and Tanaka, I., A helical string of alternately connected two three-helix bundles for the 1.1-Megadalton cell wall-associated adhesion protein Ebh from Staphylococcus aureus. Structure, 16, 488-496, (2008)
  8. Ui, M., Tanaka, Y., Tsumuraya, T., Fujii, I., Inoue, M., Hirama, M., and Tsumoto, K., How Protein Recognizes Ladder-Like Polycyclic Ethers: Interactions Between Ciguatoxin (CTX3C) Fragments and Its Specific Antibody 10C9 J. Biol. Chem., 283, 19440-19447 (2008)
  9. Watanabe, M., Tanaka, Y., Suenaga, A., Kuroda, M., Yao, M., Watanabe, N., Arisaka, F., Ohta, T., Tanaka, I., and Tsumoto, K., Structural basis for multimeric heme complexation through a specific protein-heme interaction: the case of the third NEAT domain of IsdH from Staphylococcus aureus, J. Biol. Chem.,283, 28649-28659 (2008)
  10. Tanaka, Y., Morikawa, K., Ohki, Y., Yao, M., Tsumoto, K., Watanabe, N., Ohta, T., and Tanaka, I., Structural and mutational analyses of Drp35 from Staphylococcus aureus: a possible mechanism for its lactonase activity. J. Biol. Chem., 282, 5770-5780 (2007)
Activities in Academic Societies
Protein Science Society of Japan, The Crystallographic Society of Japan, The Biophysical Society of Japan, The Japanese Biochemical Society

Food protein chemistry (School of Agricultural Science), Applied Biological Molecular Science Seminar (Graduate School of Life Sciences)

Recent Activities

We elucidate molecular mechanism of proteins which have important role for diseases and biology from structural point of view, particularly using X-ray crystallography. Recently, we revealed molecular mechanism of sulfur transfer enzyme responsible for RNA thiolation (Fig.1), and pore-forming toxin expressed by pathogenic bacteria (Fig.2). Furthermore, we apply the revealed molecular properties to design functional biomacromolecule.

Message to Students

As mentioned as “seeing is believing”, visualization of molecule gives us important clues to understand molecular mechanism. And, it is impressive study. I would like to share the impression with you and create a new research field.