Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/101527
Full metadata record
DC FieldValueLanguage
dc.contributor.authorLi, Yanen
dc.contributor.authorPillay, Shubhadraen
dc.contributor.authorFrolova, Ludmilaen
dc.contributor.authorPervushin, Konstantinen
dc.contributor.authorWong, Leo E.en
dc.date.accessioned2014-01-22T06:14:42Zen
dc.date.accessioned2019-12-06T20:39:57Z-
dc.date.available2014-01-22T06:14:42Zen
dc.date.available2019-12-06T20:39:57Z-
dc.date.copyright2012en
dc.date.issued2012en
dc.identifier.citationWong, 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.en
dc.identifier.urihttps://hdl.handle.net/10356/101527-
dc.description.abstractTranslation 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.en
dc.description.sponsorshipMOE (Min. of Education, S’pore)en
dc.language.isoenen
dc.relation.ispartofseriesNucleic acids researchen
dc.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.en
dc.subjectDRNTU::Science::Biological sciencesen
dc.titleSelectivity of stop codon recognition in translation termination is modulated by multiple conformations of GTS loop in eRF1en
dc.typeJournal Articleen
dc.contributor.schoolSchool of Biological Sciencesen
dc.identifier.doi10.1093/nar/gks192en
dc.description.versionPublished versionen
dc.identifier.pmid22383581-
item.grantfulltextopen-
item.fulltextWith Fulltext-
Appears in Collections:SBS Journal Articles

SCOPUSTM   
Citations 20

15
Updated on Jul 11, 2022

PublonsTM
Citations 20

14
Updated on Jul 11, 2022

Page view(s) 20

546
Updated on Aug 16, 2022

Download(s) 10

298
Updated on Aug 16, 2022

Google ScholarTM

Check

Altmetric


Plumx

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