Please use this identifier to cite or link to this item: https://doi.org/10.1038/ncomms12070
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dc.titleStructural basis of suppression of host translation termination by Moloney Murine Leukemia Virus
dc.contributor.authorTang, X
dc.contributor.authorZhu, Y
dc.contributor.authorBaker, S.L
dc.contributor.authorBowler, M.W
dc.contributor.authorChen, B.J
dc.contributor.authorChen, C
dc.contributor.authorHogg, J.R
dc.contributor.authorGoff, S.P
dc.contributor.authorSong, H
dc.date.accessioned2020-09-09T01:32:04Z
dc.date.available2020-09-09T01:32:04Z
dc.date.issued2016
dc.identifier.citationTang, 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
dc.identifier.issn20411723
dc.identifier.urihttps://scholarbank.nus.edu.sg/handle/10635/174953
dc.description.abstractRetroviral 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.
dc.publisherNature Publishing Group
dc.sourceUnpaywall 20200831
dc.subjectpeptidyl release factor 1
dc.subjectpeptidyl release factor 3
dc.subjectprotein
dc.subjectribonuclease H
dc.subjectRNA directed DNA polymerase
dc.subjectunclassified drug
dc.subjectEtf1 protein, mouse
dc.subjectGag protein
dc.subjectmessenger RNA
dc.subjectpeptide-chain-release factor 3
dc.subjectprotein binding
dc.subjecttranslation termination factor
dc.subjectcrystal structure
dc.subjecthuman immunodeficiency virus
dc.subjectmachinery
dc.subjectpeptide
dc.subjectprotein
dc.subjectvirus
dc.subjectArticle
dc.subjectcarboxy terminal sequence
dc.subjectcontrolled study
dc.subjectcrystal structure
dc.subjecthost
dc.subjectHuman immunodeficiency virus
dc.subjectMoloney murine leukemia virus
dc.subjectnonhuman
dc.subjectnonsense mediated mRNA decay
dc.subjectprotein binding
dc.subjectprotein interaction
dc.subjectstop codon
dc.subjectanimal
dc.subjectcalorimetry
dc.subjectchemistry
dc.subjectHEK293 cell line
dc.subjectHeLa cell line
dc.subjecthuman
dc.subjectmetabolism
dc.subjectMoloney murine leukemia virus
dc.subjectmouse
dc.subjectmutation
dc.subjectprotein domain
dc.subjecttranslation termination
dc.subjectMoloney murine leukemia virus
dc.subjectAnimals
dc.subjectCalorimetry
dc.subjectCodon, Terminator
dc.subjectFusion Proteins, gag-pol
dc.subjectHEK293 Cells
dc.subjectHeLa Cells
dc.subjectHIV Reverse Transcriptase
dc.subjectHumans
dc.subjectMice
dc.subjectMoloney murine leukemia virus
dc.subjectMutation
dc.subjectNonsense Mediated mRNA Decay
dc.subjectPeptide Chain Termination, Translational
dc.subjectPeptide Termination Factors
dc.subjectProtein Binding
dc.subjectProtein Domains
dc.subjectRibonuclease H
dc.subjectRNA, Messenger
dc.subjectRNA-Directed DNA Polymerase
dc.typeArticle
dc.contributor.departmentDEPT OF BIOCHEMISTRY
dc.description.doi10.1038/ncomms12070
dc.description.sourcetitleNature Communications
dc.description.volume7
dc.description.page12070
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