- Laboratory of X-Ray Structural Biology
- Research Theme
- Regulation and structure of translation and RNA processing
- Research Keywords
Structural biology, Protein crystallography, Bioinformation, Computer science, Translation, RNA, ribosome, automation of structure analysis
Overview of Research
In order to actualize the cellular function, it is common for living organisms that genetic information must be expressed into functional proteins by two stages, transcription and translation. The overall goal of our research is to understand the molecular basis and regulatory mechanism of transcription and translation system. The structural analysis coupled with biochemical experiment and in silico functional analysis is the core of our research methods.
Automating structure analysis: Recently, the advances in protein crystallography made structural analysis became a fast, easy and commonly used method. However, the more efficient, rapid and simplified process of structural analysis is still necessary to according to current research. We developed a program named LAFIRE for automating the whole process of structural refinement. We are also working on development of full automatic and intellectual structure analysis system.
Maturation process of tRNA: In the protein synthesis on the ribosome, aminoacyl-tRNA is an adapter molecule that transfers the amino acid to the polypeptide of protein corresponding to the genetic code (codon) of mRNA. After being transcribed from DNA, tRNA undergoes complicated maturation processes involving many factors to become an aminoacyl-tRNA.Such maturation processes of tRNA are involved with various biological activities of all living organisms and also various diseases. We aim at studying the mechanisms of tRNA maturation processes by structural analysis of individual factors and complexes, to elucidate life phenomena and provide useful information for drug discovery.
Combination of structural biology and computer science: We interest in combine structural biology and computer science for understanding systematically of life. We also develope the algorithm and AI technologies for functional analysis and drug design based on the 3D-structure in silicon.
- School of Science:
Biological Science course (Macromolecular Functions), Core Laboratories
- Graduate School of Life Science:
Division of Life Science, Transdisciplinary Life Science Course, Bioinformation and Molecular Sciences
Selective Recent Publications
Jian Yu, Akira Shinoda, Koji Kato ,Isao Tanaka and Min Yao, A solution-free crystal-mounting platform for native SAD, Acta Cryst., D76, 938-945 (2020)
Minghao Chen, Masato Ishizaka, Shun Narai, Masaki Horitani, Naoki Shigi, Min Yao & Yoshikazu Tanaka, The [4Fe-4S] cluster of sulfurtransferase TtuA desulfurizes TtuB during tRNA modification in Thermus thermophilus, Commun. Biol., 3, 168 (2020)
Meirong Chen, Zuoqi Gai, Chiaki Okada, Yuxin Ye, Jian Yu and Min Yao, Flexible NAD+ Binding in Deoxyhypusine Synthase Reflects the Dynamic Hypusine Modification of Translation Factor IF5A, Int. J. Mol. Sci., 21, 5509 (2020)
Long Li, Motoyasu Adachi, Jian Yu, Koji Kato, Akira Shinoda, Amdreas Ostermann, Tobias E. Schrader, Toyoyuki Ose and Min Yao, Neutron crystallographic study of heterotrimeric glutamine amidotransferase CAB, Acta Cryst., F75, 193-196 (2019)
Takehito Tanzawa, Koji Kato, Dylan Girodat, Toyoyuki Ose, Yuki Kumakura, Hans-Joachim Wieden, Toshio Uchiumi, Isao Tanaka, and Min Yao, The C-terminal helix of ribosomal P stalk recognizes a hydrophobic groove of elongation factor 2 in a novel fashion, Nucleic Acids Research, 46, 3232-3244 (2018)
Meirong Chen, Koji Kato, Yume Kubo, Yoshikazu Tanaka, Yuchen Liu, Feng Long, William Whitman, Pascal Lill, Christos Gatsogiannis, Stefan Raunser, Nobutaka Shimizu, Akira Shinoda, Akiyoshi Nakamura, Isao Tanaka, and Min Yao, Structural basis for the tRNA-dependent cysteine biosynthesis, Nature Communications, 8, 1512-1532 (2017)
Shoko Kimura, Tateki Suzuki, Meirong Chen, Koji Kato, Jian Yu, Akiyoshi Nakamura, Isao Tanaka, Min Yao, Template-dependent nucleotide addition in the reverse (3′-5′) direction by Thg1-like protein, Science Advances, 2, e1501397 (2016)
Refer to HOKKAIDO UNIVERSITY RESEARCHERS DIRECTORY
– Time: Anytime during the lecture period
– Place: Science Bldg. No.5, 3F, #5-311
Please contact in advance by E-mail.
- Faculty of Advanced Life Science, Department of Advanced Transdisciplinary Sciences, X-Ray Structural Biology
- Frontier Research Center for Advanced Material and Life Science, Advanced Facility Unit