Associate Professor, Department of Life Science
PhD 1994, Tokyo Institute of Technology
Office: Room 302C, M6 building, Ookayama campus
Areas of Research: Molecular Biology, Biophysics, Protein Sciences.
Keywords: Proteomics, Membrane Lipid Raft, NMR.
Body is composed by cells, and cells are driven by bio molecules. Bio molecules are machines made by usual atoms like proton, carbon, and nitrogen, and there is no magical materials generating mysteries of the life. Nevertheless, we actually feel something different from matters about the life phenomena like spirits. We think that secrets of the life lie in harmony of simple biological events occurring in the cells. If it is true, to reveal principles of the life, we must comprehensively look over the biological events from above. For the purpose, we have developed some novel techniques, a site directed labeling method for single molecular observations and a high performance proteomics. The former is to see migrations of components of the life system, and the latter is applicable to grasp contents of the component. Using these technologies, we are attempting to elucidate a biological system, membrane lipid raft that is supposed to function for appropriate response of the cells.
In addition, we are applying our original high performance technique to objects that conventional methods were not applicable. Because proteins regulate the life system, comprehensive grasp of condition of the whole proteins in the cells is the ultimate profiling of the life system. Nevertheless, the conventional proteomics has so far been difficult to do, and the subjects were restricted. On the other hands, our new technique has achieved high through put, high reproducibility, and high sensitivity performance. And, the fields are now expanding from basic sciences to clinical researches. We will make new field of proteomics.
- Hembram DS, Haremaki T, Hamatsu J, Inoue J, Kamoshida H, Ikeya T, Mishima M, Mikawa T, Hayashi N, Shirakawa M, Ito Y.: An in-cell NMR study of monitoring stress-induced increase of cytosolic Ca(2+) concentration in HeLa cells.. Biochem Biophys Res Commun., 438, 653-659. (2013)
- Ikeda-Boku A, Kondo K, Ohno S, Yoshida E, Yokogawa T, Hayashi N, Nishikawa K.: Protein fishing using magnetic nano-beads containing calmodulin site-specifically immobilized via an azido-group. J Biochem.,154, 159-165 (2013)
- Kakuta S., Yamamoto H., Negishi L., Kondo-Kakuta C., Hayashi N., Ohsumi Y.: ATG9 vesicles recruit vesicle-tethering proteins Trs85 and Ypt1 to the autophagosome formation site. J. Biol. Chem. 287, 44261-44269 (2012)
- Majava V, Wang C, Myllykoski M, Kangas SM, Kang SU, Hayashi N, Baumgärtel P, Heape AM, Lubec G, *Kursula P. Structural analysis of the complex between calmodulin and full-length myelin basic protein, an intrinsically disordered molecule. Amino Acids, 39, 59-71 (2012)
- Ikeya T, Sasaki A, Sakakibara D, Shigemitsu Y, Hamatsu J, Hanashima T, Mishima M, Yoshimasu M, Hayashi N, Mikawa T, Nietlispach D, Wälchli M, Smith BO, Shirakawa M, Guntert P, Ito Y . NMR protein structure determination in living E.coli cells using nonlinear sampling. Nature Prot., 5(6):1051-60 (2010)
- Hayashi N, Titani K, N-myristoylated proteins, key components in intracellular signal transduction systems enabling rapid and flexible cell responses. Proc.,Jpn.,Acad.,Ser.B, 86(5):494-508, (2010)
- Hayashi N, Takeuchi M, Nakanishi T, Hashimoto K, Dijkstra JM. Zinc-dependent binding between peptides derived from rainbow trout CD8a and LCK. Fish and Shellfish Immunology, 28(1):72-76 (2010)
- Sakakibara D, Sasaki A, Ikeya T, Hamatsu J, Hanashima T, Mishima M, Yoshimasu M, Hayashi N, Mikawa T, Walchli M, Smith BO, Shirakawa M, Guntert P, Ito Y. Protein structure determination in living cells by in-cell NMR spectroscopy. Nature, 458: 102-105 (2009)
- Asada A, Yamamoto N, Gohda M, Saito T, Hayashi N, Hisanaga S, Myristoylation of p35 and p39 as a determinant of cytoplasmic or nuclear localization of active Cdk5 complexes. J. Neurochem., 106: 1325-1336 (2008)
- Kurosawa G, Akahori Y, Morita M, Sumitomo M, Sato N, Muramatsu C, Eguchi K, Matsuda K, Takasaki A, Tanaka M, Iba Y, Hamada-Tsutsumi A, Ukai Y, Shiraishi M, Suzuki K, Kurosawa M, Fujiyama S, Takahashi N, Kato R, Mizoguchi Y, Shamoto M, Tsuda H, Sugiura M, Hattori Y, Miyakawa S, Shiroki R, Hoshinaga K, Hayashi N, Sugioka A, Kurosawa Y, Comprehensive screening for antigens overexpressed on carcinomas via isolation of human mAbs that may be therapeutic. Proc. Natl. Acad. Sci. U.S.A., 105: 7287-7292 (2008)
- Izumi Y, Watanabe H, Watanabe N, Aoyama A, Jinbo Y, Hayashi N, Solution X-ray scattering reveals a novel structure of calmodulin complexed with a binding domain peptide from the HIV-1 matrix protein p17. Biochemistry, 47: 7158-7166 (2008)
- Matsubara M, Jing T, Kawamura K, Shimojo N, Titani K, Hashimoto K, Hayashi N, Myristoyl moiety of HIV Nef is involved in regulation of the interaction with calmodulin in vivo. Protein Sci. 14: 494-503 (2005)
- Hayashi N, Nakagawa C, Takasaki A, Jinbo Y, Yamakawa Y, Titani K, Hashimoto K, Izumi Y, Matsushima N, Myristoylation-regulated direct interaction between calcium-bound calmodulin and N-terminal region of pp60v-src. J.Mol.Biol. 338: 169-180 (2004)
- Matsubara M, Titani K, Taniguchi H, Hayashi N, Direct involvement of protein myristoylation in MRACKS-calmodulin interaction. J.Biol.Chem. 278.48898-48902 (2003)