Hideaki Moriyama
Hideaki Moriyama
Associate Professor

Ph.D. Osaka Univeristy, 1987
M.S. Kumamoto Institute of Technology, 1984
B.S. Kumamoto Institute of Technology, 1982
Contact Information
243 Manter Hall



Research Interests

BIOS 237 Basic Applications of Bioinformatics (4 credits), spring semester
BIOS 427/827 Bioinformatics Laboratory (3 credits), spring semester

Structural Biology

Life in Nebraska is peaceful. In early spring, we have the annual migration of sandhill cranes and waterfowls through central Nebraska. We enjoy seasonal food from Farmers' Markets. In winter, we have crystal clear blue skies and dry cool air, which resemble space environments. Despite such a quiet neighborhood, our studies in Biological Sciences are exciting. Thanks to my colleagues and friends, I am enjoying science, touching and watching lives.

In our body, numerous metabolic chemical reactions are taking place. Proteins play a role in many chemical reactions. Hence, proteins are working as molecular machineries at the scene of life activities. Protein molecules interact with other molecules and change their shape during the process. My interest lies in how much energy is needed to change the shape, and in what is the meaning in organisms?

Leaving Japan, I arrived at the University of Nebraska-Lincoln in June 2002 as an Associate Research Professor in the Chemistry Department and the Center for Biotechnology. I moved to the School of Biological Sciences in August 2008 as an Associate Professor. Since then I have been studying proteins in an attempt to answer the above question. Since the function of a protein is determined by its shape, I have been using the protein crystallography as a microscope. It is including three properties of light, including energy, time, and phase. Since the shape of a protein is determined by its amino acid sequence, I have been taking idea of molecular evolution and population genetics.

In my studies, I will discuss about biological phenomena at the elementary level. For instance, when we investigate the fertilization barrier in terms of speciation, I chose marine invertebrates due to the visibility and simplicity. With a long-term collaboration of Dr. Midori Matsumoto at Keio University, we have been addressing roles of substances, including proteoglycans, steroids and peptide hormones, in fertilization of starfish. Although, I am studying many different proteins, hemoglobins and olfactory receptors became the center of my interests because of their critical roles in our body.

Hemoglobin carries oxygen in red blood cells. When the supply of oxygen becomes less than necessary in any part of boy, hypoxia symptom develops. Hemoglobin plays pivotal roles in these phenomena. In the study of hypoxia adaptation with hemoglobin, with Dr. Jay F. Storz, we are making a beautiful marriage between structural biology and population genetics.

Olfactory Receptors accept odor molecules and convert the stimulation into a nerve impulse, which is transmitted to the brain. The protein is located in the membrane. Therefore, structural studies are remaining the challenge. However, these studies will give the structural framework of other receptors, including CD4 and CD 155, which accept HIV and poliovirus, respectively. Collaborations with Dr. Etsuko Moriyama encourage me to continue work.

Finally, all sciences are corroborative efforts. No one can do everything. No part can be lacked to achieve the work. This is my motto. I appreciate my colleagues. Studies on male-female interactions at the protein level with Dr. Lawrence Harshman are exciting. Dr. Catherine P. Chia has introduced a very funny organism, slime mold, to me.

My science has been supported by Nebraska Tobacco Settlement Biomedical Research Development Funds, the National Institute of Health, the National Science Foundation, and the University of Nebraska-Lincoln.

Please visit my lab's Web site for the details of my studies.


•Wakabayashi-Ito, N., Doherty, O.M., Moriyama, H., Breakefield, X.O., Gusella, J.F., O’Donnell, J.M., & Ito1, N. (2011) dtorsin, the Drosophila ortholog of the early-onset dystonia TOR1A (DYT1), plays a novel role in dopamine metabolism. PLoS ONE. in press

•Badalucco, L., Poudel, I., Yamanishi, M., Natarajan, N., & Moriyama, H. (2011). Crystallization ofChlorella deoxyuridine triphosphatase. Acta Crystallographica Section F. in press

• Natarajan, C., Jiang, X., Fago, A., Weber, R. E., Moriyama, H. & Storz, J. F. (2011). Expression and Purification of Recombinant Hemoglobin in Escherichia coli. PLos One 6, e20176.
• Naruse, N., Ishikawa, R., Sakaya, H., Moriyama, H., Hoshi, M. & Matsumoto, M. (2011). Novel conserved structural domains of acrosome reaction-inducing substance are widespread in invertebrates. Molecular Reproduction and Development 78, 57-66.
• Storz, J. F., Hoffmann, F. G., Opazo, J. C., Sanger, T. J. & Moriyama, H. (2011). Developmental regulation of hemoglobin synthesis in the green anole lizard Anolis carolinensis. J Exp Biol 214, 575-81.
• Opiyo, S. O., Pardy, R. L., Moriyama, H. & Moriyama, E. N. (2010). Evolution of the Kdo2-lipid A biosynthesis in bacteria. BMC Evol Bio Accepted.
• Zhang, H., Tully, D. C., Zhang, T., Moriyama, H., Thompson, J. & Wood, C. (2010). Molecular determinants of HIV-1 subtype C coreceptor transition from R5 to R5X4. Virology 407, 68-79.
• Storz, J. F., Runck, A. M., Moriyama, H., Weber, R. E. & Fago, A. (2010). Genetic differences in hemoglobin function between highland and lowland deer mice. J Exp Biol 213, 2565-74.
• Hassan, Y. I., Moriyama, H. & Zempleni, J. (2010). The polypeptide Syn67 interacts physically with human holocarboxylase synthetase, but is not a target for biotinylation. Arch Biochem Biophys 495, 35-41.
• Campbell, K. L., Storz, J. F., Signore, A. V., Moriyama, H., Catania, K. C., Payson, A. P., Bonaventura, J., Stetefeld, J. & Weber, R. E. (2010). Molecular basis of a novel adaptation to hypoxic-hypercapnia in a strictly fossorial mole. BMC Evol Biol 10, 214.
• Storz, J. F., Runck, A. M., Sabatino, S. J., Kelly, J. K., Ferrand, N., Moriyama, H., Weber, R. E. & Fago, A. (2009). Evolutionary and functional insights into the mechanism underlying high-altitude adaptation of deer mouse hemoglobin. Proc Natl Acad Sci U S A 106, 14450-5.
• Runck, A. M., Moriyama, H. & Storz, J. F. (2009). Evolution of duplicated beta-globin genes and the structural basis of hemoglobin isoform differentiation in Mus. Mol Biol Evol 26, 2521-32.
• Homma, K. & Moriyama, H. (2009). Crystallization and crystal-packing studies of Chlorella virus deoxyuridine triphosphatase. Acta Cryst. F65, 1030-1034.
• Hassan, Y. I., Moriyama, H., Olsen, L. J., Bi, X. & Zempleni, J. (2009). N- and C-terminal domains in human holocarboxylase synthetase participate in substrate recognition. Mol Genet Metab 96, 183-8.
• Storz, J. F. & Moriyama, H. (2008). Mechanisms of hemoglobin adaptation to high altitude hypoxia. High Alt Med Biol 9, 148-57.
• Storz, J. F., Hoffmann, F. G., Opazo, J. C. & Moriyama, H. (2008). Adaptive Functional Divergence Among Triplicated alpha-Globin Genes in Rodents. Genetics 178, 1623-38.
• Nakachi, M., Matsumoto, M., Terry, P. M., Cerny, R. L. & Moriyama, H. (2008). Identification of guanylate cyclases and related signaling proteins in sperm tail from sea stars by mass spectrometry. Mar Biotechnol (NY) 10, 564-71.
• Nakachi, M., Hoshi, M., Matsumoto, M. & Moriyama, H. (2008). Conserved sequences of sperm-activating peptide and its receptor throughout evolution, despite speciation in the sea star Asterias amurensis and closely related species. Zygote 16, 229-37.
• Casas-Mollano, J. A., Jeong, B. R., Xu, J., Moriyama, H. & Cerutti, H. (2008). The MUT9p kinase phosphorylates histone H3 threonine 3 and is necessary for heritable epigenetic silencing in Chlamydomonas. Proc Natl Acad Sci U S A 105, 6486-91.
• Storz, J., Sabatino, S., Gering, E., Moriyama, H., Ferrand, N., Montiero, B. & Nachman, N. (2007). The molecular basis of high-altitude adaptation in deer mice PLoS Genetics 3, 448-459.
• Bajaj, M. & Moriyama, H. (2007). Purification, crystallization and preliminary crystallographic analysis of deoxyuridine triphosphate nucleotidohydrolase from Arabidopsis thaliana. Acta Cryst. F63, 409-411.
• Xu, W., Ahmed, S., Moriyama, H. & Chollet, R. (2006). The Importance of the Strictly Conserved, C-terminal Glycine Residue in Phosphoenolpyruvate Carboxylase for Overall Catalysis: MUTAGENESIS AND TRUNCATION OF GLY-961 IN THE SORGHUM C4 LEAF ISOFORM. J Biol Chem 281, 17238-45.
• Nakachi, M., Moriyama, H., Hoshi, M. & Matsumoto, M. (2006). Acrosome reaction is subfamily specific in sea star fertilization. Dev Biol 298, 597-604.
• Alvarez-Venegas, R., Sadder, M., Hlavacka, A., Baluska, F., Xia, Y., Lu, G., Firsov, A., Sarath, G., Moriyama, H., Dubrovsky, J. G. & Avramova, Z. (2006). The Arabidopsis homolog of trithorax, ATX1, binds phosphatidylinositol 5-phosphate, and the two regulate a common set of target genes. Proc Natl Acad Sci U S A 103, 6049-54.
• Abdelnoor, R. V., Christensen, A. C., Mohammed, S., Munoz-Castillo, B., Moriyama, H. & Mackenzie, S. A. (2006). Mitochondrial genome dynamics in plants and animals: convergent gene fusions of a MutS homologue. J Mol Evol 63, 165-73.
• Zhang, Y., Moriyama, H., Homma, K. & Van Etten, J. L. (2005). Chlorella virus-encoded deoxyuridine triphosphatases exhibit different temperature optima. J Virol 79, 9945-53.