Please use this identifier to cite or link to this item:
https://doi.org/10.1038/ncomms12070
DC Field | Value | |
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dc.title | Structural basis of suppression of host translation termination by Moloney Murine Leukemia Virus | |
dc.contributor.author | Tang, X | |
dc.contributor.author | Zhu, Y | |
dc.contributor.author | Baker, S.L | |
dc.contributor.author | Bowler, M.W | |
dc.contributor.author | Chen, B.J | |
dc.contributor.author | Chen, C | |
dc.contributor.author | Hogg, J.R | |
dc.contributor.author | Goff, S.P | |
dc.contributor.author | Song, H | |
dc.date.accessioned | 2020-09-09T01:32:04Z | |
dc.date.available | 2020-09-09T01:32:04Z | |
dc.date.issued | 2016 | |
dc.identifier.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 | |
dc.identifier.issn | 20411723 | |
dc.identifier.uri | https://scholarbank.nus.edu.sg/handle/10635/174953 | |
dc.description.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. | |
dc.publisher | Nature Publishing Group | |
dc.source | Unpaywall 20200831 | |
dc.subject | peptidyl release factor 1 | |
dc.subject | peptidyl release factor 3 | |
dc.subject | protein | |
dc.subject | ribonuclease H | |
dc.subject | RNA directed DNA polymerase | |
dc.subject | unclassified drug | |
dc.subject | Etf1 protein, mouse | |
dc.subject | Gag protein | |
dc.subject | messenger RNA | |
dc.subject | peptide-chain-release factor 3 | |
dc.subject | protein binding | |
dc.subject | translation termination factor | |
dc.subject | crystal structure | |
dc.subject | human immunodeficiency virus | |
dc.subject | machinery | |
dc.subject | peptide | |
dc.subject | protein | |
dc.subject | virus | |
dc.subject | Article | |
dc.subject | carboxy terminal sequence | |
dc.subject | controlled study | |
dc.subject | crystal structure | |
dc.subject | host | |
dc.subject | Human immunodeficiency virus | |
dc.subject | Moloney murine leukemia virus | |
dc.subject | nonhuman | |
dc.subject | nonsense mediated mRNA decay | |
dc.subject | protein binding | |
dc.subject | protein interaction | |
dc.subject | stop codon | |
dc.subject | animal | |
dc.subject | calorimetry | |
dc.subject | chemistry | |
dc.subject | HEK293 cell line | |
dc.subject | HeLa cell line | |
dc.subject | human | |
dc.subject | metabolism | |
dc.subject | Moloney murine leukemia virus | |
dc.subject | mouse | |
dc.subject | mutation | |
dc.subject | protein domain | |
dc.subject | translation termination | |
dc.subject | Moloney murine leukemia virus | |
dc.subject | Animals | |
dc.subject | Calorimetry | |
dc.subject | Codon, Terminator | |
dc.subject | Fusion Proteins, gag-pol | |
dc.subject | HEK293 Cells | |
dc.subject | HeLa Cells | |
dc.subject | HIV Reverse Transcriptase | |
dc.subject | Humans | |
dc.subject | Mice | |
dc.subject | Moloney murine leukemia virus | |
dc.subject | Mutation | |
dc.subject | Nonsense Mediated mRNA Decay | |
dc.subject | Peptide Chain Termination, Translational | |
dc.subject | Peptide Termination Factors | |
dc.subject | Protein Binding | |
dc.subject | Protein Domains | |
dc.subject | Ribonuclease H | |
dc.subject | RNA, Messenger | |
dc.subject | RNA-Directed DNA Polymerase | |
dc.type | Article | |
dc.contributor.department | DEPT OF BIOCHEMISTRY | |
dc.description.doi | 10.1038/ncomms12070 | |
dc.description.sourcetitle | Nature Communications | |
dc.description.volume | 7 | |
dc.description.page | 12070 | |
Appears in Collections: | Elements Staff Publications |
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