Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/101527
Title: Selectivity of stop codon recognition in translation termination is modulated by multiple conformations of GTS loop in eRF1
Authors: Li, Yan
Pillay, Shubhadra
Frolova, Ludmila
Pervushin, Konstantin
Wong, Leo E.
Keywords: DRNTU::Science::Biological sciences
Issue Date: 2012
Source: Wong, L. E., Li, Y., Pillay, S., Frolova, L., & Pervushin, K. (2012). Selectivity of stop codon recognition in translation termination is modulated by multiple conformations of GTS loop in eRF1. Nucleic acids research, 40(12), 5751-5765.
Series/Report no.: Nucleic acids research
Abstract: Translation termination in eukaryotes is catalyzed by two release factors eRF1 and eRF3 in a cooperative manner. The precise mechanism of stop codon discrimination by eRF1 remains obscure, hindering drug development targeting aberrations at translation termination. By solving the solution structures of the wild-type N-domain of human eRF1 exhibited omnipotent specificity, i.e. recognition of all three stop codons, and its unipotent mutant with UGA-only specificity, we found the conserved GTS loop adopting alternate conformations. We propose that structural variability in the GTS loop may underline the switching between omnipotency and unipotency of eRF1, implying the direct access of the GTS loop to the stop codon. To explore such feasibility, we positioned N-domain in a pre-termination ribosomal complex using the binding interface between N-domain and model RNA oligonucleotides mimicking Helix 44 of 18S rRNA. NMR analysis revealed that those duplex RNA containing 2-nt internal loops interact specifically with helix α1 of N-domain, and displace C-domain from a non-covalent complex of N-domain and C-domain, suggesting domain rearrangement in eRF1 that accompanies N-domain accommodation into the ribosomal A site.
URI: https://hdl.handle.net/10356/101527
http://hdl.handle.net/10220/18690
DOI: 10.1093/nar/gks192
Rights: © 2012 The Authors. This paper was published in Nucleic Acids Research and is made available as an electronic reprint (preprint) with permission of the authors. The paper can be found at the following official DOI: [http://dx.doi.org/10.1093/nar/gks192]. One print or electronic copy may be made for personal use only. Systematic or multiple reproduction, distribution to multiple locations via electronic or other means, duplication of any material in this paper for a fee or for commercial purposes, or modification of the content of the paper is prohibited and is subject to penalties under law.
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SBS Journal Articles

Google ScholarTM

Check

Altmetric


Plumx

Items in DR-NTU are protected by copyright, with all rights reserved, unless otherwise indicated.