Structural basis of tRNA agmatinylation essential for AUA codon decoding

Takuo Osawa, Satoshi Kimura, Naohiro Terasaka, Hideko Inanaga, Tsutomu Suzuki, Tomoyuki Numata

研究成果: ジャーナルへの寄稿学術誌査読

18 被引用数 (Scopus)

抄録

The cytidine at the first position of the anticodon (C34) in the AUA codon-specific archaeal tRNA Ile2 is modified to 2-agmatinylcytidine (agm 2 C or agmatidine), an agmatine-conjugated cytidine derivative, which is crucial for the precise decoding of the genetic code. Agm 2 C is synthesized by tRNA Ile-agm 2 C synthetase (TiaS) in an ATP-dependent manner. Here we present the crystal structures of the Archaeoglobus fulgidus TiaS-tRNA Ile2 complexed with ATP, or with AMPCPP and agmatine, revealing a previously unknown kinase module required for activating C34 by phosphorylation, and showing the molecular mechanism by which TiaS discriminates between tRNA Ile2 and tRNA Met. In the TiaS-tRNA Ile2-ATP complex, C34 is trapped within a pocket far away from the ATP-binding site. In the agmatine-containing crystals, C34 is located near the AMPCPP γ-phosphate in the kinase module, demonstrating that agmatine is essential for placing C34 in the active site. These observations also provide the structural dynamics for agm 2 C formation.

本文言語英語
ページ(範囲)1275-1280
ページ数6
ジャーナルNature Structural and Molecular Biology
18
11
DOI
出版ステータス出版済み - 11月 2011
外部発表はい

!!!All Science Journal Classification (ASJC) codes

  • 構造生物学
  • 分子生物学

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