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TitleCryo-EM structure of a mammalian RNA polymerase II elongation complex inhibited by α-amanitin.
Journal, issue, pagesJ Biol Chem, Vol. 293, Issue 19, Page 7189-7194, Year 2018
Publish dateMay 11, 2018
AuthorsXiangyang Liu / Lucas Farnung / Christoph Wigge / Patrick Cramer /
PubMed AbstractRNA polymerase II (Pol II) is the central enzyme that transcribes eukaryotic protein-coding genes to produce mRNA. The mushroom toxin α-amanitin binds Pol II and inhibits transcription at the step ...RNA polymerase II (Pol II) is the central enzyme that transcribes eukaryotic protein-coding genes to produce mRNA. The mushroom toxin α-amanitin binds Pol II and inhibits transcription at the step of RNA chain elongation. Pol II from yeast binds α-amanitin with micromolar affinity, whereas metazoan Pol II enzymes exhibit nanomolar affinities. Here, we present the high-resolution cryo-EM structure of α-amanitin bound to and inhibited by its natural target, the mammalian Pol II elongation complex. The structure revealed that the toxin is located in a pocket previously identified in yeast Pol II but forms additional contacts with metazoan-specific residues, which explains why its affinity to mammalian Pol II is ∼3000 times higher than for yeast Pol II. Our work provides the structural basis for the inhibition of mammalian Pol II by the natural toxin α-amanitin and highlights that cryo-EM is well suited to studying interactions of a small molecule with its macromolecular target.
External linksJ Biol Chem / PubMed:29550768 / PubMed Central
MethodsEM (single particle)
Resolution3.6 Å
Structure data

3981

6exv

EMDB-3981, PDB-6exv:
Structure of mammalian RNA polymerase II elongation complex inhibited by Alpha-amanitin
Method: EM (single particle) / Resolution: 3.6 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-MG:
Unknown entry

Source
  • sus scrofa (pig)
  • synthetic construct (others)
  • amanita phalloides (death cap)
KeywordsTRANSCRIPTION / Inhibitor / elongation / active site

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