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TitleStructural basis for sequence-independent substrate selection by eukaryotic wobble base tRNA deaminase ADAT2/3.
Journal, issue, pagesNat Commun, Vol. 13, Issue 1, Page 6737, Year 2022
Publish dateNov 8, 2022
AuthorsLuciano G Dolce / Aubree A Zimmer / Laura Tengo / Félix Weis / Mary Anne T Rubio / Juan D Alfonzo / Eva Kowalinski /
PubMed AbstractThe 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.
External linksNat Commun / PubMed:36347890 / PubMed Central
MethodsEM (single particle)
Resolution3.6 Å
Structure data

15690

8aw3

EMDB-15690, PDB-8aw3:
Cryo-EM structure of the Tb ADAT2/3 deaminase in complex with tRNA
Method: EM (single particle) / Resolution: 3.6 Å

Chemicals

ChemComp-ZN:
Unknown entry

Source
  • trypanosoma brucei brucei (eukaryote)
  • trypanosoma brucei (eukaryote)
KeywordsRNA BINDING PROTEIN / ADAT; inosine; tRNA modification; deaminase; cryo-EM structure; Trypanosoma brucei

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