論文

査読有り
2008年7月

Molecular basis for maintenance of fidelity during the CCA-adding reaction by a CCA-adding enzyme

EMBO JOURNAL
  • Yukimatsu Toh
  • ,
  • Tomoyuki Numata
  • ,
  • Kazunori Watanabe
  • ,
  • Daijiro Takeshita
  • ,
  • Osamu Nureki
  • ,
  • Kozo Tomita

27
14
開始ページ
1944
終了ページ
1952
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1038/emboj.2008.124
出版者・発行元
NATURE PUBLISHING GROUP

CCA-adding enzyme builds the 3'-end CCA of tRNA without a nucleic acid template. The mechanism for the maintenance of fidelity during the CCA-adding reaction remains elusive. Here, we present almost a dozen complex structures of the class I CCA-adding enzyme and tRNA mini-helices (mini-D(73)N(74), mini-D(73)N(74)C(75) and mini-D(73)C(74)N(75); D(73) is a discriminator nucleotide and N is either A, G, or U). The mini-D(73)N(74) complexes adopt catalytically inactive open forms, and CTP shifts the enzymes to the active closed forms and allows N(74) to flip for CMP incorporation. In contrast, unlike the catalytically active closed form of the mini-D(73)C(74)C(75) complex, the mini-D(73)N(74)C(75) and mini-D(73)C(74)N(75) complexes adopt inactive open forms. Only the mini-D(73)C(74)U(75) accepts AMP to a similar extent as mini-D(73)C(74)C(75), and ATP shifts the enzyme to a closed, active form and allows U(75) to flip for AMP incorporation. These findings suggest that the 3'-region of RNA is proofread, after two nucleotide additions, in the closed, active form of the complex at the AMP incorporation stage. This proofreading is a prerequisite for the maintenance of fidelity for complete CCA synthesis.

Web of Science ® 被引用回数 : 24

リンク情報
DOI
https://doi.org/10.1038/emboj.2008.124
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000257881800003&DestApp=WOS_CPL

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