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| Title | Structure of the 80S ribosome-Xrn1 nuclease complex. |
|---|---|
| Journal, issue, pages | Nat Struct Mol Biol, Vol. 26, Issue 4, Page 275-280, Year 2019 |
| Publish date | Mar 25, 2019 |
 Authors | Petr Tesina / Elisabeth Heckel / Jingdong Cheng / Micheline Fromont-Racine / Robert Buschauer / Lukas Kater / Birgitta Beatrix / Otto Berninghausen / Alain Jacquier / Thomas Becker / Roland Beckmann /   |
| PubMed Abstract | Messenger RNA (mRNA) homeostasis represents an essential part of gene expression, in which the generation of mRNA by RNA polymerase is counter-balanced by its degradation by nucleases. The conserved ...Messenger RNA (mRNA) homeostasis represents an essential part of gene expression, in which the generation of mRNA by RNA polymerase is counter-balanced by its degradation by nucleases. The conserved 5'-to-3' exoribonuclease Xrn1 has a crucial role in eukaryotic mRNA homeostasis by degrading decapped or cleaved mRNAs post-translationally and, more surprisingly, also co-translationally. Here we report that active Xrn1 can directly and specifically interact with the translation machinery. A cryo-electron microscopy structure of a programmed Saccharomyces cerevisiae 80S ribosome-Xrn1 nuclease complex reveals how the conserved core of Xrn1 enables binding at the mRNA exit site of the ribosome. This interface provides a conduit for channelling of the mRNA from the ribosomal decoding site directly into the active center of the nuclease, thus separating mRNA decoding from degradation by only 17 ± 1 nucleotides. These findings explain how rapid 5'-to-3' mRNA degradation is coupled efficiently to its final round of mRNA translation. |
 External links | Nat Struct Mol Biol / PubMed:30911188 |
| Methods | EM (single particle) |
| Resolution | 3.1 Å |
| Structure data | |
| Chemicals |  ChemComp-ZN:  ChemComp-MG: |
| Source |
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 Keywords |  TRANSLATION / ribosome / stalling / nuclease / exoribonuclease / Xrn1 |
