Headline News

Assistant Professor Position: Lab. of Cell Systems

●Details for the application



●Deadline of the application:Wednesday, January 15, 2020 (Japan Standard Time)


Inquiry on the position

Mariko Okada
Professor of Laboratory of Institute for Protein Research,
Chairman of Selection Committee

Tel: +81-(0)6-6879-8617
E-mail: mokada[a]protein.osaka-u.ac.jp (change [a] to @)

Publication:”An Assembly Intermediate Structure of Rice Dwarf Virus Reveals a Hierarchical Outer Capsid Shell Assembly Mechanism”

Dr. Yusuke Nakamichi, Mr. Kenta Tsutsumi, Dr. Akifumi Higashiura of Nakagawa Lab. and Dr. Naoyuki Miyazaki of Takagi Lab. and their collaborators revealed intermediate structure during self-assembly process of Rice dwarf virus using cryo-electron microscopy with phase plate.

   Many viruses are covered with shells of proteins that have an icosahedral structure which are known for the pattern of a soccer ball. The Reoviridae viruses have a distinctive structure further covered with a multilayered shell (capsid) of a different pattern. Rotavirus that causes infant diarrhea is well known as an example. We succeeded to reveal the formation of multilayered capsids with different patterns in Rice Dwarf Virus (RDV), one of the Reoviridae viruses, by genetic engineering technology and phase-contrast cryo-electron microscopy.

   RDV is covered with icosahedral capsids of two different patterns called T = 1 (inner shell) and T = 13 (outer capsid). In this study, we coupled green fluorescent protein (GFP) to the outer capsid protein using genetic recombination technology and used it to form virus particles. As a result, RDV particles with an incomplete shell was created by the sterically hinderance of GFP. A phase-contrast cryo-electron microscopy revealed that the outer capsid proteins of RDV bind only to a specific region of the inner capsid (on the three-fold axes). It was found that the outer shell protein of RDV is firstly bound on the three-rotational axes of the inner shell, and other pouter capsid proteins are sequentially inserted on the beside of the initially bound proteins so as to combine the pieces of the puzzle.

   This result revealed how the reovirus particles with multilayered shells are formed for the first time. In addition, by using this result to efficiently inhibit particle formation, it is expected to be applicable to the prevention of infectious diseases and development of therapeutic drugs. This research project was conducted in collaboration with Dr. Kazuyoshi Murata of National Institute for Physiological Sciences. Okazaki, Japan.

An Assembly Intermediate Structure of Rice Dwarf Virus Reveals a Hierarchical Outer Capsid Shell Assembly Mechanism, Yusuke Nakamichi, Naoyuki Miyazaki, Kenta Tsutsumi, Akifumi Higashiura, Hirotaka Narita, Kazuyoshi Murata, Atsushi Nakagawa, Structure, 27(3), 439-448, 2019
doi: https://doi.org/10.1016/j.str.2018.10.029

This paper is downloadable from the following URL until April 24, 2019.


Registration for the IPR 60th Anniversary International Symposium has started.

Registration for the IPR 60th Anniversary International Syposium has started.

Please go to the 60th anversary event website to register.


Date:Friday, November 16, 2018

Venue: Room Senju, Senri Hankyu Hotel












●Invited Speakers:

・Yoshinori Ohsumi (2016 Nobel Laureate, Honorary Professor, Tokyo Institute of Technology)
・Richard Henderson (2017 Nobel Laureate, MRC Laboratory of Molecular Biology)
・Bong-Jin Lee (Dean, College of Pharmacy, Seoul National University
・Yoshihiro Yoneda (Director General and Project Leader, National Institutes of Biomedical Innovation, Health and Nutrition)
・Atsushi Miyawaki (Laboratory Head, RIKEN Center for Brain Science(CBS) )




Institute for Protein Research, Osaka University

3-2 Yamadaoka, Suita, Osaka, Japan
TEL: 06-6879-8601/Fax: 06-6879-8603
Email: j-60kinen[at]protein.osaka-u.ac.jp


The earthquake that struck northern Osaka on June 18

No faculty members, students and staff at IPR were injured by the earthquake that struck northern Osaka on Monday, June 18.

However, there was severe damage on facilities and equipment including NMR, microscopes, DNA sequencers, and FACS at some laboratories of IPR.

We would like to express our appreciation for messages of concern and warm words of encouragement, and ask for your continued support moving forward.


Prof. Mariko Okada was awarded the 2018 Commendations for Science and Technology by MEXT

The Ministry of Education, Culture, Sports, Science and Technology (MEXT)announced the recipients of the 2018 Commendations for Science and Technology. From Osaka University, eight faculty member received awards, including Prof. Mariko Okada of Institute for Protein Research.

Prof. Okada was awarded the Prize for Science and Technology (Research Category).

Name of Achievement: Research on cellular mechanisms based on experiments and mathematical models


Website of Osaka Univ.



Click here for more datails on Prof. Okada’s research

Publication:“Phosphorylation of an intrinsically disordered region of Ets1 shifts a multi-modal interaction ensemble to an auto-inhibitory state”

On 4th January 2018, a paper has been published from Nucleic Acids Research (IF=10.162) by the research team of Dr. Kota Kasahara (Ritsumeikan University), Dr. Masaaki Shiina, Prof. Kazuhiro Ogata (Yokohama City University), Prof. Junichi Higo and Prof. Haruki Nakamura (IPR, Osaka University), revealing the regulation mechanism of the intrinsically disordered region of Ets1 transcription factor due to phosphorylation of Ser residues by molecular simulation and biochemical studies.


Click here for more details


Science Agora 2017 -in Tokyo-

IPR, together with PDBj, Hiroshima City Univ.Ritsumeikan Univ. and Kwansei Gakuin Univ. will hold a booth at Science Agora 2017 organized by Japan Science and Technology Agancy (JST).

  • November 24 (Friday), 2017 (13:30〜18:00)
  • November 25 (Saturday) – November 26 (Sunday) (10:00〜16:00)
Telecom Center Building, Odaiba Tokyo
5th floor Area D (innovating new knowledge by linking different fields), Booth No.65

“Shape” of proteins, which supporting the life

(The website linked from the title is displayed only in Japanese)
The aim of our exhibition is providing chances for various people to realize the diversity and importance of the “Shape” of proteins though experiences such as watching, feeling and constructing. We hope it helps them to deepen their understanding for biomolecules. The details of exhibition are as following:
  1. “Watching” by accessing PDBj database and browsing protein molecules with CG in sterically.
  2. “Feeling” by touching the molecule models made with a 3D printer
  3. “Constructing” by making molecules with paper crafts
We also introduce the methods and facilities such as synchrotrons and high resolution electron microscopes (Nobel Prize of this year was awarded for it!) to solve molecule shapes.