Structural basis of suppression of host translation termination by Moloney Murine Leukemia Virus

Xuhua Tang, Yiping Zhu, Stacey L. Baker, Matthew W. Bowler, Benjamin Jieming Chen, Chen Chen, J. Robert Hogg (), Stephen P. Goff () and Haiwei Song ()
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Xuhua Tang: Institute of Molecular and Cell Biology
Yiping Zhu: Columbia University
Stacey L. Baker: Biochemistry and Biophysics Center, National Heart, Lung, and Blood Institute, National Institutes of Health
Matthew W. Bowler: European Molecular Biology Laboratory, Grenoble Outstation
Benjamin Jieming Chen: Institute of Molecular and Cell Biology
Chen Chen: Institute of Molecular and Cell Biology
J. Robert Hogg: Biochemistry and Biophysics Center, National Heart, Lung, and Blood Institute, National Institutes of Health
Stephen P. Goff: Columbia University
Haiwei Song: Institute of Molecular and Cell Biology

Nature Communications, 2016, vol. 7, issue 1, 1-10

Abstract: 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.

Date: 2016
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DOI: 10.1038/ncomms12070

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