Novel Function of Protein; Regulation of Enzymatic Activities; Molecular Evolution; Protein Engineering; Molecular Design; Biochemistry; Molecular Biology; Hemoprotein; Aminoacyl-tRNA Synthetase; Protein; Enzyme; Angiogenesis; Neuroprotection.

Investigation of novel function of neuroglobin

Investigation of novel function of aminoacyl-tRNA synthetase

Creation of artificial functional proteins

Graduate students: 8

Undergraduates: 1

Secretary & technichan: 0

1. Watanabe, S., and Wakasugi, K. Zebrafish neuroglobin is a cell-membrane-penetrating globin. Biochemistry 47, 5266-5270 (2008).

2. Watanabe, S., and Wakasugi, K. Neuroprotective function of human neuroglobin is correlated with its guanine nucleotide dissociation inhibitor activity. Biochem. Biophys. Res. Commun 369, 695-700 (2008).

3. Ishikawa, H., Kim, S., Kwak, K., Wakasugi, K., and Fayer, M. D. Disulfide bond influence on protein structural dynamics probed with 2D-IR vibrational echo spectroscopy. Proc. Natl. Acad. Sci. USA 104, 19309-19314 (2007).

4. Ishikawa, H., Finkelstein, I. J., Kim, S., Kwak, K., Chung, J. K., Wakasugi, K., Massari, A. M., and Fayer, M. D. Neuroglobin dynamics observed with ultrafast 2D-IR vibrational echo spectroscopy. Proc. Natl. Acad. Sci. USA 104, 16116-16121 (2007).

5. Wakasugi, K. Human tryptophanyl-tRNA synthetase binds with heme to enhance its aminoacylation activity. Biochemistry 46, 11291-11298 (2007).

6. Kitatsuji, C., Kurogochi, M., Nishimura, S.-I., Ishimori, K., and Wakasugi, K. Molecular basis of guanine nucleotide dissociation inhibitor activity of human neuroglobin by chemical cross-linking and mass spectrometry. J. Mol. Biol. 368, 150-160 (2007).

7. Wakasugi, K., Kitatsuji, C., and Morishima, I. Possible neuroprotective mechanism of human neuroglobin. Ann. N.Y. Acad. Sci. 1053, 220-230 (2005).

8. Wakasugi, K., and Morishima, I. Preparation and characterization of a chimeric zebrafish-human neuroglobin engineered by module substitution. Biochem. Biophys. Res. Commun. 330, 591-597 (2005).

9. Wakasugi, K., and Morishima, I. Identification of residues in human neuroglobin crucial for guanine nucleotide dissociation inhibitor activity. Biochemistry 44, 2943-2948 (2005).

10. Wakasugi, K., Nakano, T., and Morishima, I. Oxidative stress-responsive intracellular regulation specific for the angiostatic form of human tryptophanyl-tRNA synthetase. Biochemistry 44, 225-232 (2005).

11. Wakasugi, K., Nakano, T., and Morishima, I. Association of human neuroglobin with cystatin C, a cysteine proteinase inhibitor. Biochemistry (Accelerated Publication) 43, 5119-5125 (2004).

12. Wakasugi, K., Nakano, T., Kitatsuji, C., and Morishima, I. Human neuroglobin interacts with flotillin-1, a lipid raft microdomain-associated protein. Biochem. Biophys. Res. Commun. 318, 453-460 (2004).

13. Wakasugi, K., Nakano, T., and Morishima, I. Oxidized human neuroglobin acts as a heterotrimeric Galpha protein guanine nucleotide dissociation inhibitor. J. Biol. Chem. 278, 36505-36512 (2003).

14. Wakasugi, K., Slike, B. M., Hood, J., Ewalt, K. L., Cheresh, D. A., and Schimmel, P. Induction of angiogenesis by a fragment of human tyrosyl-tRNA synthetase. J. Biol. Chem. (Accelerated Publication) 277, 20124-20126 (2002).

15. Wakasugi, K., Slike, B. M., Hood, J., Otani, A., Ewalt, K. L., Friedlander, M., Cheresh, D. A., and Schimmel, P. A human aminoacyl-tRNA synthetase as a regulator of angiogenesis. Proc. Natl. Acad. Sci. USA 99, 173-177 (2002).

16. Wakasugi, K., and Schimmel, P. Highly differentiated motifs responsible for two cytokine activities of a split human tRNA synthetase. J. Biol. Chem. 274, 23155-23159 (1999).

17. Wakasugi, K., and Schimmel, P. (1999) Two distinct cytokines released from a human aminoacyl-tRNA synthetase. Science 284, 147-151.

18. Wakasugi, K., Quinn, C., Tao, N., and Schimmel, P. Genetic code in evolution: switching species-specific aminoacylation with a peptide transplant. EMBO J. 17, 297-305 (1998).

19. Wakasugi, K., Ishimori, K., and Morishima, I. "Module"-substituted globins: Artificial exon shuffling among myoglobin, hemoglobin α- and β-subunits. Biophys. Chem. 68, 265-273 (1997).

20. Inaba, K., Wakasugi, K., Ishimori, K., Konno, T., Kataoka, M., and Morishima, I. Structural and functional roles of modules in hemoglobin: substitution of module M4 in hemoglobin subunits. J. Biol. Chem. 272, 30054-30060 (1997).

21. Wakasugi, K., Ishimori, K., and Morishima, I. NMR Studies of Recombinant Cytochrome P450cam Mutants. Biochimie 78, 763-770 (1996).

22. Wakasugi, K., Ishimori, K., and Morishima, I. Module Substitution in Globins. Preparation and Association Characteristics of Chimeric Hemoglobin Subunits and Myoglobin. Tracing Biological Evolution in Protein and Gene Structures (eds. Go, M. & Schimmel, P.) , Elsevier, 283-295 (1995).

23. Wakasugi, K., Ishimori, K., Imai, K., Wada, Y., and Morishima, I. "Module" Substitution in Hemoglobin Subunits: Preparation and Characterization of a "Chimera βα-Subunit". J. Biol. Chem. 269, 18750-18756 (1994).

24. Watanabe, S., and Wakasugi, K. Module M1 of zebrafish neuroglobin acts as a structural and functional protein building block for a cell-membrane-penetrating activity. PLoS ONE 6, e16808 (2011).