Structural Biology Laboratory

Structural Biology Laboratory

SelA

We focus our studies on the central dogma of molecular biology, "DNA makes RNA makes protein", which are the processes of duplication (DNA → DNA), transcription (DNA → RNA), and translation (RNA → protein). We investigate the mechanisms underlying the extremely high specificities of these processes, with regard to the four bases and the twenty amino acids common to all organisms, at the level of the three-dimensional structures of protein•nucleic acid complexes by X-ray crystallographic structural studies. Furthermore, on the basis of the three-dimensional structures, we construct central dogma systems expanded with unnatural bases and amino acids. This combination of analytical and synthetic approaches allows us not only to understand the physicochemical mechanisms of the high specificities in the natural central dogma, but also to develop new biotechnologies with the distinct advantages of the unnatural bases and amino acids.

Press Release

 
  • SARS-CoV 3CL protease cleaves its C-terminal autoprocessing site by novel subsite cooperativity Journal: Proc. Natl. Acad. Sci. U.S.A. 

 
 
  • Essential components for cell viability

    *Japanese only

    Researchers led by Drs. Shigeyuki Yokoyama and Tatsuo Yanagisawa revealed the translation elongation factor P (EF-P) and the Arg residue at position 32 are constituent elements of the cell viability of a human pathogen, Neisseria meningitides.

 
  • Overall structure of the eukaryotic translation initiation 2B (eIF2B), revealed

    *Japanese only

    Researchers led by Drs. Shigeyuki Yokoyama and Takuhiro Ito have successfully determined the structure of the eIF2B and unveiled its structural framework for the eIF2B associated mechanism of the pathogenesis of vanishing white matter (VWM) or childhood ataxia with central nervous system hypomyelination (CACH).

 
 
 
  • Structure of RNA Polymerase, revealed

    Researchers led by Drs. Shigeyuki Yokoyama and Shun-ichi Sekine have shown that the conversion between the tight and ratcheted forms could be the general basis for the regulation of RNAP functions in all cellular multisubunit RNAPs.

 
  • Redox switch in Lon protease, revealed

    Researchers led by Drs. Shigeyuki Yokoyama and Wataru Nishii have discovered that Lon protease is regulated by a redox-dependent disulfide bond that determines the size of its exit pore.



 
  • Structure of alanyl-tRNA synthetase, revealed

    Researchers led by Dr. Shigeyuki Yokoyama have determined the crystal structure of alanyl-tRNA synthetase and elucidated astonishing selective tRNA aminoacylation mechanisms.

 
  • Structure of SelA, the 21st amino acid synthase, revealed

    Researchers led by Dr. Shigeyuki Yokoyama have determined the crystal structure of the Sec synthase, SelA, responsible for the Ser-to-Sec conversion in bacteria. They determined the structures of SelA alone and in a complex with tRNASec.

News

 
 
  • The Commendation for Science and Technology

    Dr. Shigeyuki Yokoyama was awarded The Commendation for Science and Technology by the Minister of Education, Culture, Sports, Science and Technology (Prize for Science and Technology) in 2014.