Molecular basis of translation termination at noncanonical stop codons in human mitochondria-Reference-Cited by-同舟云学术

Molecular basis of translation termination at noncanonical stop codons in human mitochondria

Published:2023-05-05 Issue:6644 Volume:380 Page:531-536
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Saurer Martin¹^ORCID,Leibundgut Marc¹^ORCID,Nadimpalli Hima Priyanka²^ORCID,Scaiola Alain¹^ORCID,Schönhut Tanja¹^ORCID,Lee Richard G.³⁴⁵^ORCID,Siira Stefan J.³⁴^ORCID,Rackham Oliver³⁴⁵⁶^ORCID,Dreos René²^ORCID,Lenarčič Tea¹^ORCID,Kummer Eva⁷^ORCID,Gatfield David²^ORCID,Filipovska Aleksandra³⁴⁵^ORCID,Ban Nenad¹^ORCID

Affiliation:

1. Department of Biology, Institute of Molecular Biology and Biophysics, ETH Zürich, 8093 Zürich, Switzerland.

2. Center for Integrative Genomics, University of Lausanne, 1015 Lausanne, Switzerland.

3. Harry Perkins Institute of Medical Research, The University of Western Australia, Nedlands, Western Australia 6009, Australia.

4. ARC Centre of Excellence in Synthetic Biology, QEII Medical Centre, The University of Western Australia, Nedlands, Western Australia 6009, Australia.

5. Telethon Kids Institute, Northern Entrance, Perth Children's Hospital, 15 Hospital Avenue, Nedlands, Western Australia, Australia.

6. Curtin Medical School and Curtin Health Innovation Research Institute, Curtin University, Bentley, Western Australia 6102, Australia.

7. Novo Nordisk Foundation Center for Protein Research, Protein Structure and Function Program, Blegdamsvej 3B, 2200 København N, Denmark.

Abstract

The genetic code that specifies the identity of amino acids incorporated into proteins during protein synthesis is almost universally conserved. Mitochondrial genomes feature deviations from the standard genetic code, including the reassignment of two arginine codons to stop codons. The protein required for translation termination at these noncanonical stop codons to release the newly synthesized polypeptides is not currently known. In this study, we used gene editing and ribosomal profiling in combination with cryo–electron microscopy to establish that mitochondrial release factor 1 (mtRF1) detects noncanonical stop codons in human mitochondria by a previously unknown mechanism of codon recognition. We discovered that binding of mtRF1 to the decoding center of the ribosome stabilizes a highly unusual conformation in the messenger RNA in which the ribosomal RNA participates in specific recognition of the noncanonical stop codons.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Link

https://www.science.org/doi/pdf/10.1126/science.adf9890

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