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TitleMolecular basis of tRNA recognition by the Elongator complex.
Journal, issue, pagesSci Adv, Vol. 5, Issue 7, Page eaaw2326, Year 2019
Publish dateJul 10, 2019
AuthorsMaria I Dauden / Marcin Jaciuk / Felix Weis / Ting-Yu Lin / Carolin Kleindienst / Nour El Hana Abbassi / Heena Khatter / Rościsław Krutyhołowa / Karin D Breunig / Jan Kosinski / Christoph W Müller / Sebastian Glatt /
PubMed AbstractThe highly conserved Elongator complex modifies transfer RNAs (tRNAs) in their wobble base position, thereby regulating protein synthesis and ensuring proteome stability. The precise mechanisms of ...The highly conserved Elongator complex modifies transfer RNAs (tRNAs) in their wobble base position, thereby regulating protein synthesis and ensuring proteome stability. The precise mechanisms of tRNA recognition and its modification reaction remain elusive. Here, we show cryo-electron microscopy structures of the catalytic subcomplex of Elongator and its tRNA-bound state at resolutions of 3.3 and 4.4 Å. The structures resolve details of the catalytic site, including the substrate tRNA, the iron-sulfur cluster, and a SAM molecule, which are all validated by mutational analyses in vitro and in vivo. tRNA binding induces conformational rearrangements, which precisely position the targeted anticodon base in the active site. Our results provide the molecular basis for substrate recognition of Elongator, essential to understand its cellular function and role in neurodegenerative diseases and cancer.
External linksSci Adv / PubMed:31309145 / PubMed Central
MethodsEM (single particle)
Resolution3.3 - 6.7 Å
Structure data

4571

6qk7

EMDB-4571, PDB-6qk7:
Elongator catalytic subcomplex Elp123 lobe
Method: EM (single particle) / Resolution: 3.3 Å

EMDB-4573:
Full Elongator catalytic subcomplex Elp123
Method: EM (single particle) / Resolution: 4.5 Å

EMDB-4574:
tRNA-bound Elongator catalytic subcomplex, tRNA-Elp123 lobe.
Method: EM (single particle) / Resolution: 4.4 Å

EMDB-4576:
2tRNAs-bound Elongator catalytic subcomplex, 2tRNA-Elp123.
Method: EM (single particle) / Resolution: 6.7 Å

Chemicals

ChemComp-SF4:
IRON/SULFUR CLUSTER / Iron–sulfur cluster

ChemComp-5AD:
5'-DEOXYADENOSINE / Deoxyadenosine

Source
  • Saccharomyces cerevisiae (brewer's yeast)
  • Baker's yeast (brewer's yeast)
  • saccharomyces cerevisiae (strain atcc 204508 / s288c) (yeast)
KeywordsTRANSLATION / Elongator / yeast / tRNA modification / Elp123

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