Conformational changes in Lassa virus L protein associated with promoter binding and RNA synthesis activity

The L protein of segmented, negative strand RNA viruses contains the RNA-dependent RNA polymerase essential for virus amplification. Here, the authors report cryoEM structures of the Lassa virus L protein in active, RNA-bound states, and provide mechanistic insights.

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Autores principales: Tomas Kouba, Dominik Vogel, Sigurdur R. Thorkelsson, Emmanuelle R. J. Quemin, Harry M. Williams, Morlin Milewski, Carola Busch, Stephan Günther, Kay Grünewald, Maria Rosenthal, Stephen Cusack
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Publicado: Nature Portfolio 2021
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Acceso en línea:https://doaj.org/article/97a04e7215a44a4ebaec52c71bff412e
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spelling oai:doaj.org-article:97a04e7215a44a4ebaec52c71bff412e2021-12-05T12:22:47ZConformational changes in Lassa virus L protein associated with promoter binding and RNA synthesis activity10.1038/s41467-021-27305-52041-1723https://doaj.org/article/97a04e7215a44a4ebaec52c71bff412e2021-12-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-27305-5https://doaj.org/toc/2041-1723The L protein of segmented, negative strand RNA viruses contains the RNA-dependent RNA polymerase essential for virus amplification. Here, the authors report cryoEM structures of the Lassa virus L protein in active, RNA-bound states, and provide mechanistic insights.Tomas KoubaDominik VogelSigurdur R. ThorkelssonEmmanuelle R. J. QueminHarry M. WilliamsMorlin MilewskiCarola BuschStephan GüntherKay GrünewaldMaria RosenthalStephen CusackNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-18 (2021)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Tomas Kouba
Dominik Vogel
Sigurdur R. Thorkelsson
Emmanuelle R. J. Quemin
Harry M. Williams
Morlin Milewski
Carola Busch
Stephan Günther
Kay Grünewald
Maria Rosenthal
Stephen Cusack
Conformational changes in Lassa virus L protein associated with promoter binding and RNA synthesis activity
description The L protein of segmented, negative strand RNA viruses contains the RNA-dependent RNA polymerase essential for virus amplification. Here, the authors report cryoEM structures of the Lassa virus L protein in active, RNA-bound states, and provide mechanistic insights.
format article
author Tomas Kouba
Dominik Vogel
Sigurdur R. Thorkelsson
Emmanuelle R. J. Quemin
Harry M. Williams
Morlin Milewski
Carola Busch
Stephan Günther
Kay Grünewald
Maria Rosenthal
Stephen Cusack
author_facet Tomas Kouba
Dominik Vogel
Sigurdur R. Thorkelsson
Emmanuelle R. J. Quemin
Harry M. Williams
Morlin Milewski
Carola Busch
Stephan Günther
Kay Grünewald
Maria Rosenthal
Stephen Cusack
author_sort Tomas Kouba
title Conformational changes in Lassa virus L protein associated with promoter binding and RNA synthesis activity
title_short Conformational changes in Lassa virus L protein associated with promoter binding and RNA synthesis activity
title_full Conformational changes in Lassa virus L protein associated with promoter binding and RNA synthesis activity
title_fullStr Conformational changes in Lassa virus L protein associated with promoter binding and RNA synthesis activity
title_full_unstemmed Conformational changes in Lassa virus L protein associated with promoter binding and RNA synthesis activity
title_sort conformational changes in lassa virus l protein associated with promoter binding and rna synthesis activity
publisher Nature Portfolio
publishDate 2021
url https://doaj.org/article/97a04e7215a44a4ebaec52c71bff412e
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