X-ray Crystallography of tRNA recycling enzyme:substrate complex

2014 Fiscal Year Final Research Report

• Project/Area Number: 24770093
• Research Category: Grant-in-Aid for Young Scientists (B)
• Allocation Type: Multi-year Fund
• Research Field: Structural biochemistry
• Research Institution: Niigata University
• Principal Investigator: ITO Kosuke 新潟大学, 自然科学系, 助教 (20502397)
• Project Period (FY): 2012-04-01 – 2015-03-31
• Keywords: ｔRNA再生酵素 / ペプチジルtRNA / 翻訳 / X線結晶構造解析

Outline of Final Research Achievements

tRNA recycling enzyme cleaves the ester bond between the peptide and the tRNA of peptidyl-tRNA molecules, which are produced by aborted translation, to recycle tRNA for further rounds of protein synthesis. Here we have determined the crystal structure of the tRNA recycling enzyme in complex with the tRNA CCA-acceptor-TΨC domain, the enzyme-binding region of the tRNA moiety of the substrate. The structure provided insights into how tRNA recycling enzyme accepts the diverse sequences of the elongator-tRNAs as substrate components. Furthermore, we proposed an authentic tRNA recycling enzyme:peptidyl-tRNA complex model, based on the present structure and the enzymatic studies’results.

Free Research Field

構造生物学