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TitleCatalytic and regulatory basis of tRNA tA modification by the KEOPS complex.
Journal, issue, pagesNat Commun, Year 2026
Publish dateMay 15, 2026
AuthorsLi Zhou / Zelin Zhang / Mengqi Jin / Dengmiao Xie / Han Wen / Eric Westhof / Dongsheng Lei / Wenhua Zhang /
PubMed AbstractN-threonylcarbamoyladenosine (tA) at tRNA position 37 is essential for translational fidelity and cellular homeostasis. The multi-subunit KEOPS complex catalyzes tA formation in Archaea and Eukarya. ...N-threonylcarbamoyladenosine (tA) at tRNA position 37 is essential for translational fidelity and cellular homeostasis. The multi-subunit KEOPS complex catalyzes tA formation in Archaea and Eukarya. Here we present cryo-EM structures of C. elegans KEOPS in its apo and tRNA-bound states. tRNA binding induces concerted conformational rearrangements, distorting the anticodon loop to project A37 into the Kae1 active site. Kae1 recognizes the conserved G10-C25 pair and 36-UAA-38 motif. Bud32 directly contacts the anticodon and acceptor arms, coupling ATP hydrolysis to tA catalysis in the distant Kae1 active site through long-range conformational changes. Cgi121 enhances catalytic efficiency through cooperative binding with Bud32 and the tRNA 3' CCA. Pcc1 stabilizes the anticodon loop and mediates KEOPS dimerization, enhancing tRNA binding and tA activity. GAMOS-associated mutations cluster at functional hotspots within the KEOPS-tRNA complex. This study provides a structural framework for understanding KEOPS mechanism and its cellular roles.
External linksNat Commun / PubMed:42140986
MethodsEM (single particle)
Resolution3.1 - 3.36 Å
Structure data

66544

9x4g

EMDB-66544, PDB-9x4g:
Structure Of the KEOPS dimer
Method: EM (single particle) / Resolution: 3.1 Å

66545

9x4h

EMDB-66545, PDB-9x4h:
Structure Of the KEOPS-tRNA
Method: EM (single particle) / Resolution: 3.36 Å

Chemicals

ChemComp-K:
Unknown entry

Source
  • caenorhabditis elegans (invertebrata)
KeywordsTRANSFERASE / tRNA modification / t6A / KEOPS-tRNA complex / cryo-EM structure / substrate recognition / catalytic mechanism / regulation principle / TRANSFERASE/RNA / TRANSFERASE-RNA complex

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