Shin-ichi Tate has got his Ph.D. degree from the University of Tokyo in 1993. He experienced visiting researcher at ETH (Prof. K. Wühtrich) and NIH (Dr. A. Bax). He has been a professor in the department of the mathematical and life sciences at Hiroshima since 2006. He is now the director of the Research Center for the Mathematics on Chromatin live Dynamics (RcMcd), and the dean of the school of science in Hiroshima University.



The functionally relevant inter-domain communication between the domains linked by intrinsically disordered region (IDR) was explored by NMR in combination with small angle X-ray scattering (SAXS). Based on the ensemble structure analyses and the numerical simulations to reproduce the chemical shift changes along with the substrate concentration, we have demonstrated how the domains cooperate to enhance the protein function through the substantially dynamic spatial allocation of the domains.

Pin1, a proline cis/trans isomerase, comprises two domains linked by 10-residue IDR; one is the substrate biding domain to recognize pSer/pThr-Pro motif and the other is the enzyme domain that rotates the Pro peptide bond in the motif. The enzyme domain shows very limited affinity to the substrate, but its binding ability was enhanced by two orders of magnitude in the presence of the substrate binding domain linked by IDR; in which the inter-domain ‘fly-casting’ mechanism plays to keep the substrate bound to Pin1 by tossing and receiving the substrate between the domains, once the substrate in bound to either one of the domains. A new functional aspect of IDR will be addressed.


  1. Tochio,N., Umehara,K., Uewaki,J., Flechsig,H., Kondo,M., Dewa,T., Sakumar,T., Yamamoto,T., Saitoh,T, Togashi,Y., and Tate,S. (2016): Non-RVD mutations that enhance the dynamics of the TAL repeat array along the superhelical axis improve TALEN genome editing efficacy, Scientific Reports, 6, 37887.
  2. Wang,J., Tochio,N., Kawasaki,R., Tamari,Y., Xu,N., Uewaki,J., Utsunomiya-Tate, N., and Tate,S. (2015): Allosteric breakage of the hydrogen bond within the dual-histidine motif in the active site of human Pin1 PPIase, Biochemistry, 54, 5242-5253.
  3. Xu,N. Tochio,N., Wang,J., Tamari,Y., Uewaki,J. Utsunomiya-Tate,N., Igarashi,K., Shiraki,T., Kobayashi,N., and Tate,S. (2014): The C113D mutation in human Pin1 causes allosteric structural changes in the phosphate binding pocket of the PPIase domain through the tug of war in the dualhistidine motif, Biochemistry, 53, 5568-5578.
  4. Hashimoto,M., Kodera,N., Tsunaka,Y., Oda,M., Tanimoto,M., Ando,T., Morikawa,K., and Tate,S. (2013): Phosphorylation-coupled intramolecular dynamics of unstructured regions in chromatin remodeler FACT, Biophys,J. 104, 2222-2234.
  5. Mizuno, S., Amida, H., Kobayashi, N., Aizawa, S. and Tate, S. (2011): The NMR structure of FliK, the trigger for the switch of substrate specificity in the flagellar type Ⅲ secretion apparatus. J. Mol. Biol., 409, 558-573