- Laboratory of Biological Information Analysis Science
- Research Theme
- Study on structure-function relationship of biological molecules in the biomembrane system based on experimental and information sciences
- Research Keywords
Membrane protein, Peptide, Structure-function relationship, Folding, NMR, Photobiology, Rhodopsin, Apoptosis, Bioinformation, SDGs
Overview of Research
Structure and function of rhodopsin family
The seven transmembrane (7TM) receptors have a remarkable similarity to bacteriorhodopsin and halorhodopsin. These are a light driven proton pump and a light driven chloride pump from the archaebacteria. The 7TM segments enclose a retinal attached to a lysine residue of the last helix by a Schiffs base. This retinal undergoes an all-trans to 13-cis isomerization when it absorbs a photon. The conformational change is transmitted to the protein and it is used to pump protons or chloride and form a gradient. In vertebrate eyes, the protein rhodopsin is also a 7TM segment protein with retinal attached to a lysine also in the last helix. In this protein the photo-conformational change activates a signal transducer. We are investigated mechanism of ion pumping and signal transduction of archaeal rhodopsins using a transgenic technology and various spectroscopies including CD, flash-photolysis, and NMR.
Determination and prediction of protein structure using NMR and bioinformatics
The lifescience in recent years has been transfigured to the science that handles huge information by the result of the genome analysis project. It is very important to develop how to process these huge information and apply to an individual research of biomolecules such as protein, nucleic acid and biomembrane. On the other hand, advanced NMR techniques for determination of protein structure have been developed. Based on these experimental and information sciences, the methodology for determination and simulation of protein structure is developed.
Industrial application of Life Science and sustainable development goals (SDGs)
- School of Science:
Biological Science course (Macromolecular Functions), Core Laboratories
- Graduate School of Life Science:
Division of Soft Matter, Biomolecular Soft Matter
Takashi Tsukamoto, Chihiro Kikuchi, Hiromu Suzuki, Tomoyasu Aizawa,Takashi Kikukawa & Makoto Demura, Implications for the impairment of the rapid channel closing of Proteomonas sulcata anion channelrhodopsin 1 at high Cl− concentration, Scientific Reports, 8:13445 (2018)
Gang Dai, Xiong Geng, Chaoluomeng, J. Tamogami, T. Kikukawa, M. Demura, N. Kamo, T. Iwasa, Photocycle of Sensory Rhodopsin II from Halobacterium salinarum (HsSRII): Mutation of D103 Accelerates M Decay and Changes the Decay Pathway of a 13‐cis O‐like Species, Photochemistry and Photobiology, 94, 705–714 (2018)
Tamogami, T. Kikukawa, K. Ohkawa, N. Ohsawa, T. Nara, M. Demura, S. Miyauchi, T. Kimura-Someya, M. Shirouzu, S. Yokoyama, K. Shimono, N. Kamo, Interhelical interactions between D92 and C218 in the cytoplasmic domain regulate proton uptake upon N-decay in the proton transport of Acetabularia rhodopsin II, Journal of Photochemistry & Photobiology, B: Biology183, 35-45 (2018)
Nakajima, T. Tsukamoto, Y. Kumagai, Y. Ogura, T. Hayashi, J. Song, T. Kikukawa, M. Demura, K. Kogure, Y. Sudo, S. Yoshizawa, Presence of a Haloarchaeal Halorhodopsin-Like Cl- Pump in Marine Bacteria, Microbes Environ. , 2018 Mar 16.
Md. Ruhul Kuddus, Megumi Yamano, Farhana Rumi, Takashi Kikukawa, Makoto Demura, Tomoyasu Aizawa, Enhanced expression of cysteine-rich antimicrobial peptide snakin-1 in Escherichia coli using an aggregation-prone protein coexpression system, Biotechnology progress, 2017 May 27.
Refer to HOKKAIDO UNIVERSITY RESEARCHERS DIRECTORY
– Time: Anytime during the lecture period
– Place: Science Bldg. No.2, 8F, #2-805
Please contact in advance by E-mail.
- Faculty of Advanced Life Science, Department of Functional Life Sciences, Biological Information Analysis Science
- Frontier Research Center for Advanced Material and Life Science, Global Collaboration Unit, Soft Matter Collaborative Research Unit