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Takamasa Teramoto Last modified date:2021.06.24

Assistant Professor / Department of Bioresource and Bioenvironment
Department of Bioscience and Biotechnology
Faculty of Agriculture




Homepage
https://kyushu-u.pure.elsevier.com/en/persons/takamasa-teramoto
 Reseacher Profiling Tool Kyushu University Pure
Academic Degree
Ph.D.(Systems Life Sciences)
Country of degree conferring institution (Overseas)
No
Field of Specialization
Structural Biology
ORCID(Open Researcher and Contributor ID)
0000-0003-1555-5394
Total Priod of education and research career in the foreign country
08years00months
Research
Research Interests
  • The Structural biology of RNA-binding proteins and sulfotransferases
    keyword : Structural biology
    2020.02.
Academic Activities
Papers
1. Teramoto T., b,Kaitany K.J., Kakuta Y., Kimura M., Fierke C.A., Hall T.M.T., Pentatricopeptide repeats of protein-only RNase P use a distinct mode to recognize conserved bases and structural elements of pre-tRNA, Nucleic Acids Research, 10.1093/nar/gkaa627, 2020.12, Pentatricopeptide repeat (PPR) motifs are α-helical structures known for their modular recognition of single-stranded RNA sequences with each motif in a tandem array binding to a single nucleotide. Protein-only RNase P 1 (PRORP1) in Arabidopsis thaliana is an endoribonuclease that uses its PPR domain to recognize precursor tRNAs (pre-tRNAs) as it catalyzes removal of the 5′-leader sequence from pre-tRNAs with its NYN metallonuclease domain. To gain insight into the mechanism by which PRORP1 recognizes tRNA, we determined a crystal structure of the PPR domain in complex with yeast tRNAPhe at 2.85 Å resolution. The PPR domain of PRORP1 bound to the structurally conserved elbow of tRNA and recognized conserved structural features of tRNAs using mechanisms that are different from the established single-stranded RNA recognition mode of PPR motifs. The PRORP1 PPR domain-tRNAPhe structure revealed a conformational change of the PPR domain upon tRNA binding and moreover demonstrated the need for pronounced overall flexibility in the PRORP1 enzyme conformation for substrate recognition and catalysis. The PRORP1 PPR motifs have evolved strategies for protein-tRNA interaction analogous to tRNA recognition by the RNA component of ribonucleoprotein RNase P and other catalytic RNAs, indicating convergence on a common solution for tRNA substrate recognition..