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TitleRecognition and cleavage mechanism of intron-containing pre-tRNA by human TSEN endonuclease complex.
Journal, issue, pagesNat Commun, Vol. 14, Issue 1, Page 6071, Year 2023
Publish dateSep 28, 2023
AuthorsLing Yuan / Yaoyao Han / Jiazheng Zhao / Yixiao Zhang / Yadong Sun /
PubMed AbstractRemoval of introns from transfer RNA precursors (pre-tRNAs) occurs in all living organisms. This is a vital phase in the maturation and functionality of tRNA. Here we present a 3.2 Å-resolution cryo- ...Removal of introns from transfer RNA precursors (pre-tRNAs) occurs in all living organisms. This is a vital phase in the maturation and functionality of tRNA. Here we present a 3.2 Å-resolution cryo-EM structure of an active human tRNA splicing endonuclease complex bound to an intron-containing pre-tRNA. TSEN54, along with the unique regions of TSEN34 and TSEN2, cooperatively recognizes the mature body of pre-tRNA and guides the anticodon-intron stem to the correct position for splicing. We capture the moment when the endonucleases are poised for cleavage, illuminating the molecular mechanism for both 3' and 5' cleavage reactions. Two insertion loops from TSEN54 and TSEN2 cover the 3' and 5' splice sites, respectively, trapping the scissile phosphate in the center of the catalytic triad of residues. Our findings reveal the molecular mechanism for eukaryotic pre-tRNA recognition and cleavage, as well as the evolutionary relationship between archaeal and eukaryotic TSENs.
External linksNat Commun / PubMed:37770519 / PubMed Central
MethodsEM (single particle)
Resolution3.19 Å
Structure data

35694

8iss

EMDB-35694, PDB-8iss:
Cryo-EM structure of wild-type human tRNA Splicing Endonuclease Complex bound to pre-tRNA-ARG at 3.19 A resolution
Method: EM (single particle) / Resolution: 3.19 Å

Chemicals

ChemComp-MG:
Unknown entry

Source
  • homo sapiens (human)
KeywordsSTRUCTURAL PROTEIN / tRNA splicing / TSEN / Cryo-EM / endonuclease

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