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Unusual base pairing during the decoding of a stop codon by the ribosome

DOI: 10.1038/nature12302 DOI Help
PMID: 23812587 PMID Help

Authors: Israel S. Fernandez (MRC Laboratory of Molecular Biology) , Chyan Leong Ng (MRC Laboratory of Molecular Biology) , Ann C. Kelley (MRC Laboratory of Molecular Biology) , Guowei Wu (University of Rochester Medical Center) , Yi-tao Yu (University of Rochester Medical Center) , V. Ramakrishnan (MRC Laboratory of Molecular Biology)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nature , VOL 500 (7460) , PAGES 107 - 110

State: Published (Approved)
Published: June 2013

Open Access Open Access

Abstract: During normal translation, the binding of a release factor to one of the three stop codons (UGA, UAA or UAG) results in the termination of protein synthesis. However, modification of the initial uridine to a pseudouridine (Ψ) allows efficient recognition and read-through of these stop codons by a transfer RNA (tRNA), although it requires the formation of two normally forbidden purine–purine base pairs1. Here we determined the crystal structure at 3.1 Å resolution of the 30S ribosomal subunit in complex with the anticodon stem loop of tRNASer bound to the ΨAG stop codon in the A site. The ΨA base pair at the first position is accompanied by the formation of purine–purine base pairs at the second and third positions of the codon, which show an unusual Watson–Crick/Hoogsteen geometry. The structure shows a previously unsuspected ability of the ribosomal decoding centre to accommodate non-canonical base pairs.

Journal Keywords: Base; Codon; Terminator; Crystallography; X-Ray; Models; Molecular; Nucleic; Protein; Pseudouridine; RNA; Transfer; Ser; Ribosome; Small; Bacterial; Ribosomes

Subject Areas: Biology and Bio-materials

Instruments: I04-Macromolecular Crystallography

Other Facilities: beamline X06SA at the Swiss Light Source. beamline ID14-4, ESRF

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