Please use this identifier to cite or link to this item: https://doi.org/10.1038/ncomms12070
Title: Structural basis of suppression of host translation termination by Moloney Murine Leukemia Virus
Authors: Tang, X
Zhu, Y
Baker, S.L
Bowler, M.W
Chen, B.J
Chen, C
Hogg, J.R
Goff, S.P
Song, H 
Keywords: peptidyl release factor 1
peptidyl release factor 3
protein
ribonuclease H
RNA directed DNA polymerase
unclassified drug
Etf1 protein, mouse
Gag protein
messenger RNA
peptide-chain-release factor 3
protein binding
translation termination factor
crystal structure
human immunodeficiency virus
machinery
peptide
protein
virus
Article
carboxy terminal sequence
controlled study
crystal structure
host
Human immunodeficiency virus
Moloney murine leukemia virus
nonhuman
nonsense mediated mRNA decay
protein binding
protein interaction
stop codon
animal
calorimetry
chemistry
HEK293 cell line
HeLa cell line
human
metabolism
Moloney murine leukemia virus
mouse
mutation
protein domain
translation termination
Moloney murine leukemia virus
Animals
Calorimetry
Codon, Terminator
Fusion Proteins, gag-pol
HEK293 Cells
HeLa Cells
HIV Reverse Transcriptase
Humans
Mice
Moloney murine leukemia virus
Mutation
Nonsense Mediated mRNA Decay
Peptide Chain Termination, Translational
Peptide Termination Factors
Protein Binding
Protein Domains
Ribonuclease H
RNA, Messenger
RNA-Directed DNA Polymerase
Issue Date: 2016
Publisher: Nature Publishing Group
Citation: Tang, X, Zhu, Y, Baker, S.L, Bowler, M.W, Chen, B.J, Chen, C, Hogg, J.R, Goff, S.P, Song, H (2016). Structural basis of suppression of host translation termination by Moloney Murine Leukemia Virus. Nature Communications 7 : 12070. ScholarBank@NUS Repository. https://doi.org/10.1038/ncomms12070
Abstract: Retroviral reverse transcriptase (RT) of Moloney murine leukemia virus (MoMLV) is expressed in the form of a large Gag-Pol precursor protein by suppression of translational termination in which the maximal efficiency of stop codon read-through depends on the interaction between MoMLV RT and peptidyl release factor 1 (eRF1). Here, we report the crystal structure of MoMLV RT in complex with eRF1. The MoMLV RT interacts with the C-terminal domain of eRF1 via its RNase H domain to sterically occlude the binding of peptidyl release factor 3 (eRF3) to eRF1. Promotion of read-through by MoMLV RNase H prevents nonsense-mediated mRNA decay (NMD) of mRNAs. Comparison of our structure with that of HIV RT explains why HIV RT cannot interact with eRF1. Our results provide a mechanistic view of how MoMLV manipulates the host translation termination machinery for the synthesis of its own proteins.
Source Title: Nature Communications
URI: https://scholarbank.nus.edu.sg/handle/10635/174953
ISSN: 20411723
DOI: 10.1038/ncomms12070
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