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TitleStructure of a human translation termination complex.
Journal, issue, pagesNucleic Acids Res, Vol. 43, Issue 18, Page 8615-8626, Year 2015
Publish dateOct 15, 2015
AuthorsSarah Matheisl / Otto Berninghausen / Thomas Becker / Roland Beckmann /
PubMed AbstractIn contrast to bacteria that have two release factors, RF1 and RF2, eukaryotes only possess one unrelated release factor eRF1, which recognizes all three stop codons of the mRNA and hydrolyses the ...In contrast to bacteria that have two release factors, RF1 and RF2, eukaryotes only possess one unrelated release factor eRF1, which recognizes all three stop codons of the mRNA and hydrolyses the peptidyl-tRNA bond. While the molecular basis for bacterial termination has been elucidated, high-resolution structures of eukaryotic termination complexes have been lacking. Here we present a 3.8 Å structure of a human translation termination complex with eRF1 decoding a UAA(A) stop codon. The complex was formed using the human cytomegalovirus (hCMV) stalling peptide, which perturbs the peptidyltransferase center (PTC) to silence the hydrolysis activity of eRF1. Moreover, unlike sense codons or bacterial stop codons, the UAA stop codon adopts a U-turn-like conformation within a pocket formed by eRF1 and the ribosome. Inducing the U-turn conformation for stop codon recognition rationalizes how decoding by eRF1 includes monitoring geometry in order to discriminate against sense codons.
External linksNucleic Acids Res / PubMed:26384426 / PubMed Central
MethodsEM (single particle)
Resolution3.8 Å
Structure data

3099

5a8l

EMDB-3099: Cryo-EM structure of a human translation termination complex
PDB-5a8l: Human eRF1 and the hCMV nascent peptide in the translation termination complex
Method: EM (single particle) / Resolution: 3.8 Å

Source
  • homo sapiens (human)
KeywordsTRANSLATION / HUMAN / 80S / RIBOSOME / ERF1

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