Mechanisms of the tRNA wobble cytidine modification essential for AUA codon decoding in prokaryotes

研究成果: Contribution to journalReview article査読

5 被引用数 (Scopus)

抄録

Bacteria and archaea have 2-lysylcytidine (L or lysidine) and 2-agmatinylcytidine (agm (agm2C or agmatidine), respectively, at the first (wobble) position of the anticodon of the AUA codon-specific tRNAIle. These lysine- or agmatine-conjugated cytidine derivatives are crucial for the precise decoding of the genetic code. L is synthesized by tRNA tRNAelI-lysidine synthetase (TilS), which uses L-lysine and ATP as substrates. Agm2C formation is catalyzed by tRNAelI-agm2C synthetase (TiaS), which uses agmatine and ATP for the reaction. Despite the fact that TilS and TiaS synthesize structurally similar cytidine derivatives, these enzymes belong to nonrelated protein families. Therefore, these enzymes modify the wobble cytidine by distinct catalytic mechanisms, in which TilS activates the C2 carbon of the wobble cytidine by adenylation, while TiaS activates it by phosphorylation. In contrast, TilS and TiaS share similar tRNA recognition mechanisms, in which the enzymes recognize the tRNA acceptor stem to discriminate tRNAIle and tRNAMet.

本文言語英語
ページ(範囲)347-353
ページ数7
ジャーナルBioscience, Biotechnology and Biochemistry
79
3
DOI
出版ステータス出版済み - 2015
外部発表はい

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Analytical Chemistry
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology
  • Organic Chemistry

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