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-Structure paper
タイトル | Structural basis for sequence-independent substrate selection by eukaryotic wobble base tRNA deaminase ADAT2/3. |
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ジャーナル・号・ページ | Nat Commun, Vol. 13, Issue 1, Page 6737, Year 2022 |
掲載日 | 2022年11月8日 |
著者 | Luciano G Dolce / Aubree A Zimmer / Laura Tengo / Félix Weis / Mary Anne T Rubio / Juan D Alfonzo / Eva Kowalinski / |
PubMed 要旨 | The essential deamination of adenosine A to inosine at the wobble base is the individual tRNA modification with the greatest effects on mRNA decoding, empowering a single tRNA to translate three ...The essential deamination of adenosine A to inosine at the wobble base is the individual tRNA modification with the greatest effects on mRNA decoding, empowering a single tRNA to translate three different codons. To date, many aspects of how eukaryotic deaminases specifically select their multiple substrates remain unclear. Here, using cryo-EM, we present the structure of a eukaryotic ADAT2/3 deaminase bound to a full-length tRNA, revealing that the enzyme distorts the anticodon loop, but in contrast to the bacterial enzymes, selects its substrate via sequence-independent contacts of eukaryote-acquired flexible or intrinsically unfolded motifs distal from the conserved catalytic core. A gating mechanism for substrate entry to the active site is identified. Our multi-step tRNA recognition model yields insights into how RNA editing by A deamination evolved, shaped the genetic code, and directly impacts the eukaryotic proteome. |
リンク | Nat Commun / PubMed:36347890 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.6 Å |
構造データ | EMDB-15690, PDB-8aw3: |
化合物 | ChemComp-ZN: |
由来 |
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キーワード | RNA BINDING PROTEIN (RNA結合タンパク質) / ADAT; inosine; tRNA modification; deaminase; cryo-EM structure; Trypanosoma brucei (アダット) |