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; Haiwei Song

doi:10.1038/ncomms12070

Nature Communications (Jun 2016)

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,
Haiwei Song

Affiliations

Xuhua Tang: Institute of Molecular and Cell Biology
Yiping Zhu: Department of Biochemistry and Molecular Biophysics, 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: Department of Biochemistry and Molecular Biophysics, Columbia University
Haiwei Song: Institute of Molecular and Cell Biology

DOI: https://doi.org/10.1038/ncomms12070
Journal volume & issue: Vol. 7, no. 1
pp. 1 – 10

Abstract

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Retroviral reverse transcriptase from Moloney Murine Leukemia Virus (MoMLV) requires interaction with peptidyl release factor 1. Here, the authors report the crystal structure of this complex, and provide insights into how MoMLV uses the host translation machinery to synthesize its own proteins.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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