Laboratory for Cellular Structural Biology
Takanori KigawaD. Sci.
- E-mail：kigawa[at]riken.jpPlease replace [at] with @.
Understanding biological phenomena based on the structure and dynamics of biomolecules in cellular environments
In actual biological cellular environments, biomolecules such as proteins are working dynamically and co-operatively, generally surrounded by high concentrations of macromolecules, so-called “macromolecular crowding” and also “confined” by/in the plasma membrane and/or cellular organelles. In recent years, it has become important to directly investigate the structure and the dynamics of biomolecules in cellular environments because protein behaviors in cells are, at least in some cases, different from those in a dilute, homogeneous solution. We will elucidate cellular events at atomic resolution by analyzing structural dynamics of biomolecules in the cellular environment mainly by using NMR spectroscopy integrated with information science technologies. We will also develop and improve the technologies for sample preparation, stable-isotope labeling, NMR measurements, and data analyses in order to address the issues of low sensitivity and resolution from which NMR measurement of biomolecules in cellular environments usually suffers. In addition, based on our findings, we will develop new technologies by taking advantage of biological functions, for example, the development of technologies for bioelectricity generation based on the mechanisms of energy generation in the living cells.
Structural dynamics of biomolecules in cellular environments
Stable-isotope encoding (SiCode)
Bioelectricity generation technology
- NMR analysis of biomolecular structural dynamics in cellular environments
- Development of NMR-related technologies with information sciences
- Development of technologies for stable-isotope labeling of proteins using cell-free synthesis
- Development of technology for bioelectricity generation by taking advantage of biological functions
Main Publications List
Ito K, Murayama Y, Kurokawa Y, et al.
Real-time tracking reveals catalytic roles for the two DNA binding sites of Rad51.
Nature Communications 11. 2950 (2020) doi: 10.1038/s41467-020-16750-3
Higuchi K, Yabuki T, Ito M, Kigawa T.
Cold shock proteins improve E. coli cell-free synthesis in terms of soluble yields of aggregation-prone proteins
Biotechnology and Bioengineering (2020) doi: 10.1002/bit.27326
Kasai T, Ono S, Koshiba S, et al.
Amino-acid selective isotope labeling enables simultaneous overlapping signal decomposition and information extraction from NMR spectra
Journal of Biomolecular NMR (2020) doi: 10.1007/s10858-019-00295-9
Inomata K, Kamoshida H, Ikari M, et al.
Impact of cellular health conditions on the protein folding state in mammalian cells
Chemical Communications (Cambridge) 53(81). 11245-11248 (2017) doi: 10.1039/c7cc06004a
Advances in stable isotope assisted labeling strategies with information science
Archives of Biochemistry and Biophysics 628. 17-23 (2017) doi:10.1016/j.abb.2017.06.014
Kasai T, Nagata K, Okada M, Kigawa T.
NMR spectral analysis using prior knowledge
Journal of Physics: Conference Series 699(1). 012003 (2016) doi:10.1088/1742-6596/699/1/012003
Okamura H, Nishimura H, Nagata T, et al.
Accurate and molecular-size-tolerant NMR quantitation of diverse components in solution
Scientific Reports 6. 21742 (2016) doi:10.1038/srep21742
Shigeno-Nakazawa Y, Kasai T, Ki S, et al.
A pre-metazoan origin of the CRK gene family and co-opted signaling network
Scientific Reports 6. 34349 (2016) doi:10.1038/srep34349
Kasai T, Koshiba S, Yokoyama J, Kigawa T.
Stable isotope labeling strategy based on coding theory
Journal of Biomolecular NMR 63(2). 213-221 (2015) doi:10.1007/s10858-015-9978-8
Harada R, Tochio N, Kigawa T, et al.
Reduced native state stability in crowded cellular environment due to protein-protein interactions
Journal of the American Chemical Society 135(9). 3696-3701 (2013) doi:10.1021/ja3126992
Matsuda T, Furumoto S, Higuchi K, et al.
Rapid biochemical synthesis of C-11-labeled single chain variable fragment antibody for immuno-PET by cell-free protein synthesis
Bioorganic & Medicinal Chemistry 20(22). 6579-6582 (2012) doi:10.1016/j.bmc.2012.09.038
Akama S, Yamamura M, Kigawa T.
A Multiphysics Model of In Vitro Transcription Coupling Enzymatic Reaction and Precipitation Formation
Biophysical Journal 102(2). 221-230 (2012) doi:10.1016/j.bpj.2011.12.014
Yokoyama J, Matsuda T, Koshiba S, et al.
A practical method for cell-free protein synthesis to avoid stable isotope scrambling and dilution
Analytical Biochemistry 411(2). 223-229 (2011) doi:10.1016/j.ab.2011.01.017