Glycyl-tRNA synthetase specifically binds to the poliovirus IRES to activate translation initiation

Adaptation to the host cell environment to efficiently take-over the host cell's machinery is crucial in particular for small RNA viruses like picornaviruses that come with only small RNA genomes and replicate exclusively in the cytosol. Their Internal Ribosome Entry Site (IRES) elements are sp...

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Main Authors:	Andreev, Dmitri E., Hirnet, Juliane, Terenin, Ilya M., Dmitriev, Sergey E., Niepmann, Michael, Shatsky, Ivan N.
Format:	Online
Language:	English
Published:	Oxford University Press 2012
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3384309/

id	pubmed-3384309
recordtype	oai_dc
spelling	pubmed-33843092012-06-28 Glycyl-tRNA synthetase specifically binds to the poliovirus IRES to activate translation initiation Andreev, Dmitri E. Hirnet, Juliane Terenin, Ilya M. Dmitriev, Sergey E. Niepmann, Michael Shatsky, Ivan N. RNA Adaptation to the host cell environment to efficiently take-over the host cell's machinery is crucial in particular for small RNA viruses like picornaviruses that come with only small RNA genomes and replicate exclusively in the cytosol. Their Internal Ribosome Entry Site (IRES) elements are specific RNA structures that facilitate the 5′ end-independent internal initiation of translation both under normal conditions and when the cap-dependent host protein synthesis is shut-down in infected cells. A longstanding issue is which host factors play a major role in this internal initiation. Here, we show that the functionally most important domain V of the poliovirus IRES uses tRNAGly anticodon stem–loop mimicry to recruit glycyl-tRNA synthetase (GARS) to the apical part of domain V, adjacent to the binding site of the key initiation factor eIF4G. The binding of GARS promotes the accommodation of the initiation region of the IRES in the mRNA binding site of the ribosome, thereby greatly enhancing the activity of the IRES at the step of the 48S initiation complex formation. Moonlighting functions of GARS that may be additionally needed for other events of the virus–host cell interaction are discussed. Oxford University Press 2012-07 2012-02-28 /pmc/articles/PMC3384309/ /pubmed/22373920 http://dx.doi.org/10.1093/nar/gks182 Text en © The Author(s) 2012. Published by Oxford University Press. http://creativecommons.org/licenses/by-nc/3.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
repository_type	Open Access Journal
institution_category	Foreign Institution
institution	US National Center for Biotechnology Information
building	NCBI PubMed
collection	Online Access
language	English
format	Online
author	Andreev, Dmitri E. Hirnet, Juliane Terenin, Ilya M. Dmitriev, Sergey E. Niepmann, Michael Shatsky, Ivan N.
spellingShingle	Andreev, Dmitri E. Hirnet, Juliane Terenin, Ilya M. Dmitriev, Sergey E. Niepmann, Michael Shatsky, Ivan N. Glycyl-tRNA synthetase specifically binds to the poliovirus IRES to activate translation initiation
author_facet	Andreev, Dmitri E. Hirnet, Juliane Terenin, Ilya M. Dmitriev, Sergey E. Niepmann, Michael Shatsky, Ivan N.
author_sort	Andreev, Dmitri E.
title	Glycyl-tRNA synthetase specifically binds to the poliovirus IRES to activate translation initiation
title_short	Glycyl-tRNA synthetase specifically binds to the poliovirus IRES to activate translation initiation
title_full	Glycyl-tRNA synthetase specifically binds to the poliovirus IRES to activate translation initiation
title_fullStr	Glycyl-tRNA synthetase specifically binds to the poliovirus IRES to activate translation initiation
title_full_unstemmed	Glycyl-tRNA synthetase specifically binds to the poliovirus IRES to activate translation initiation
title_sort	glycyl-trna synthetase specifically binds to the poliovirus ires to activate translation initiation
description	Adaptation to the host cell environment to efficiently take-over the host cell's machinery is crucial in particular for small RNA viruses like picornaviruses that come with only small RNA genomes and replicate exclusively in the cytosol. Their Internal Ribosome Entry Site (IRES) elements are specific RNA structures that facilitate the 5′ end-independent internal initiation of translation both under normal conditions and when the cap-dependent host protein synthesis is shut-down in infected cells. A longstanding issue is which host factors play a major role in this internal initiation. Here, we show that the functionally most important domain V of the poliovirus IRES uses tRNAGly anticodon stem–loop mimicry to recruit glycyl-tRNA synthetase (GARS) to the apical part of domain V, adjacent to the binding site of the key initiation factor eIF4G. The binding of GARS promotes the accommodation of the initiation region of the IRES in the mRNA binding site of the ribosome, thereby greatly enhancing the activity of the IRES at the step of the 48S initiation complex formation. Moonlighting functions of GARS that may be additionally needed for other events of the virus–host cell interaction are discussed.
publisher	Oxford University Press
publishDate	2012
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3384309/
_version_	1611539373442990080

Glycyl-tRNA synthetase specifically binds to the poliovirus IRES to activate translation initiation

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