Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/81882
Title: Structural characterization of eRF1 mutants indicate a complex mechanism of stop codon recognition
Authors: Pillay, Shubhadra
Li, Yan
Wong, Leo E
Pervushin, Konstantin
Keywords: Cancer prevention
Solution-state NMR
Issue Date: 2016
Source: Pillay, S., Li, Y., Wong, L. E., & Pervushin, K. (2016). Structural characterization of eRF1 mutants indicate a complex mechanism of stop codon recognition. Scientific Reports, 6, 18644-.
Series/Report no.: Scientific Reports
Abstract: Eukarya translation termination requires the stop codon recognizing protein eRF1. In contrast to the multiple proteins required for translation termination in Bacteria, eRF1 retains the ability to recognize all three of the stop codons. The details of the mechanism that eRF1 uses to recognize stop codons has remained elusive. This study describes the structural effects of mutations in the eRF1 N-domain that have previously been shown to alter stop codon recognition specificity. Here, we propose a model of eRF1 binding to the pre-translation termination ribosomal complex that is based in part on our solution NMR structures of the wild-type and mutant eRF1 N-domains. Since structural perturbations induced by these mutations were spread throughout the protein structure, residual dipolar coupling (RDC) data were recorded to establish the long-range effects of the specific mutations, E55Q, Y125F, Q122FM(Y)F126. RDCs were recorded on 15N-labeled eRF1 N-domain weakly aligned in either 5% w/v n-octyl-penta (ethylene glycol)/octanol (C8E5) or the filamentous phage Pf1. These data indicate that the mutations alter the conformation and dynamics of the GTS loop that is distant from the mutation sites. We propose that the GTS loop forms a switch that is key for the multiple codon recognition capability of eRF1.
URI: https://hdl.handle.net/10356/81882
http://hdl.handle.net/10220/39718
ISSN: 2045-2322
DOI: 10.1038/srep18644
Rights: This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SBS Journal Articles

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