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Structure of the Vesicular Stomatitis Virus L Protein in Complex with Its Phosphoprotein Cofactor

Simon Jenni, Louis-Marie Bloyet, Ruben Diaz-Avalos, Bo Liang, Sean P. J. Whelan, Nikolaus Grigorieff, Stephen C. Harrison
doi: https://doi.org/10.1101/792960
Simon Jenni
Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA
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Louis-Marie Bloyet
Department of Microbiology, Harvard Medical School, Boston, MA 02115, USA
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Ruben Diaz-Avalos
Janelia Research Campus, Howard Hughes Medical Institute, Ashburn, VA 20147, USALa Jolla Institute for Immunology, La Jolla, CA 92037, USA
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Bo Liang
Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USADepartment of Microbiology, Harvard Medical School, Boston, MA 02115, USADepartment of Biochemistry, Rollins Research Center, Emory University School of Medicine, Atlanta, GA 30322, USA
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Sean P. J. Whelan
Department of Microbiology, Harvard Medical School, Boston, MA 02115, USA
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Nikolaus Grigorieff
Janelia Research Campus, Howard Hughes Medical Institute, Ashburn, VA 20147, USARNA Therapeutics Institute, University of Massachusetts Medical School, Worcester, MA 01605, USA
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Stephen C. Harrison
Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USAHoward Hughes Medical Institute, Harvard Medical School, Boston, MA 02115, USA
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  • For correspondence: harrison@crystal.harvard.edu
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SUMMARY

The large (L) proteins of non-segmented, negative-strand RNA viruses are multifunctional enzymes that produce capped, methylated and polyadenylated mRNAs and replicate the viral genome. A phosphoprotein (P), required for efficient RNA-dependent RNA polymerization from the viral ribonucleoprotein (RNP) template, regulates function and conformation of the L protein. We report the structure of vesicular stomatitis virus L in complex with its P cofactor determined by electron cryomicroscopy at 3.0 Å resolution, enabling us to visualize bound segments of P. The contacts of three P segments with multiple L domains show how P induces a closed, compact, initiation-competent conformation. Binding of P to L positions its N-terminal domain adjacent to a putative RNA exit channel for efficient encapsidation of newly synthesized genomes with the nucleoprotein and orients its C-terminal domain to interact with the RNP template. The model shows that a conserved tryptophan in the priming loop can support the initiating 5’-nucleotide.

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The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. All rights reserved. No reuse allowed without permission.
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Posted October 03, 2019.
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Structure of the Vesicular Stomatitis Virus L Protein in Complex with Its Phosphoprotein Cofactor
Simon Jenni, Louis-Marie Bloyet, Ruben Diaz-Avalos, Bo Liang, Sean P. J. Whelan, Nikolaus Grigorieff, Stephen C. Harrison
bioRxiv 792960; doi: https://doi.org/10.1101/792960
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Structure of the Vesicular Stomatitis Virus L Protein in Complex with Its Phosphoprotein Cofactor
Simon Jenni, Louis-Marie Bloyet, Ruben Diaz-Avalos, Bo Liang, Sean P. J. Whelan, Nikolaus Grigorieff, Stephen C. Harrison
bioRxiv 792960; doi: https://doi.org/10.1101/792960

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