Professor Hideaki Tsuge

Area and Subject Taught Structural Biology
Research Theme(s) Structural and Functional Study of Protein Complex
Academic Degrees Ph.D(Faculty of Sciences)
Keywords for Research Field Protein Crystallography,Structure,Infectious Disease
Office Phone Number 81-75-705-3117

Research Overview

We are currently pursuing the structural biology of infectious disease. I am interested in the protein-protein interactions between infectious factors and host protein. Now we are studying the next two main themes. (1) In 2008, we revealed the complex crystal structure of actin specific ADP-ribosylating toxin Ia (ADPRT) and host protein actin. Up to that time, many toxin structures were available, but there was no complex structure at all. In 2013,we revealed the pre- and post- ADP-ribosylation state of Ia-actin complex. Our structure provides the clue of ADP-ribosylation reaction between protein and protein. Now we are focusing RhoA specific ADPRT (C3 exoenzyme) and RhoA interaction (ref 4 and 3). (2) In highly pathogenic influenza, some mutations in RNA polymerase are known. Especially E627K mutant is very famous. In 2009, we revealed the crystal structure of PB2 C-terminal domain including K627. This structure provides the first insight of the reason of highly pathogenicity.

Notable Publications and Works in the Last Three Years

  1. Toniti W, Yoshida T, Tsurumura T, Irikura D, Monma C, Kamata Y, Tsuge H.Crystal structure and structure-based mutagenesis of actin-specific ADP-ribosylating toxin CPILE-a as novel enterotoxin.PLoS One. 12(2):e0171278. (2017)
  2. Tsuge H, Tsurumura T, Toda A, Murata H, Toniti W, Yoshida T.Comparative Studies of Actin- and Rho-Specific ADP-Ribosylating Toxins: Insight from Structural Biology.Curr Top Microbiol Immunol. 399:69-86. (2017)
  3. Tsuge H, Yoshida T, Tsurumura T.Conformational plasticity is crucial for C3-RhoA complex formation by ARTT-loop.Pathog Dis. 73(9):ftv094. doi: 10.1093/femspd/ftv094. Epub (2015)
  4. Toda A, Tsurumura T, Yoshida T, Tsumori Y, Tsuge H. Rho GTPase Recognition by C3 Exoenzyme Based on C3-RhoA Complex Structure. J Biol Chem. 7;290(32):19423-32. (2015)
  5. Kobayashi H, Yoshida T, Miyakawa T, Tashiro M, Okamoto K, Yamanaka H, Tanokura M, Tsuge H.: Structural Basis for Action of the External Chaperone for a Propeptide-deficient Serine Protease from Aeromonas sobria. J Biol Chem. 290 (17): 11130-43. 2015