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© Research
Publication : Nature structural & molecular biology

Structure of the 80S ribosome-Xrn1 nuclease complex

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Nature structural & molecular biology - 25 Mar 2019

Tesina P, Heckel E, Cheng J, Fromont-Racine M, Buschauer R, Kater L, Beatrix B, Berninghausen O, Jacquier A, Becker T, Beckmann R

Link to Pubmed [PMID] – 30911188

Nat. Struct. Mol. Biol. 2019 Apr;26(4):275-280

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.

https://www.ncbi.nlm.nih.gov/pubmed/30911188