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Stability of local secondary structure determines selectivity of viral RNA chaperones

JPK. Bravo, A. Borodavka, A. Barth, AN. Calabrese, P. Mojzes, JJB. Cockburn, DC. Lamb, R. Tuma,

. 2018 ; 46 (15) : 7924-7937. [pub] 20180906

Jazyk angličtina Země Anglie, Velká Británie

Typ dokumentu časopisecké články, práce podpořená grantem

Perzistentní odkaz   https://www.medvik.cz/link/bmc19035222

Grantová podpora
BB/E012558/1 Biotechnology and Biological Sciences Research Council - United Kingdom
Wellcome Trust - United Kingdom

To maintain genome integrity, segmented double-stranded RNA viruses of the Reoviridae family must accurately select and package a complete set of up to a dozen distinct genomic RNAs. It is thought that the high fidelity segmented genome assembly involves multiple sequence-specific RNA-RNA interactions between single-stranded RNA segment precursors. These are mediated by virus-encoded non-structural proteins with RNA chaperone-like activities, such as rotavirus (RV) NSP2 and avian reovirus σNS. Here, we compared the abilities of NSP2 and σNS to mediate sequence-specific interactions between RV genomic segment precursors. Despite their similar activities, NSP2 successfully promotes inter-segment association, while σNS fails to do so. To understand the mechanisms underlying such selectivity in promoting inter-molecular duplex formation, we compared RNA-binding and helix-unwinding activities of both proteins. We demonstrate that octameric NSP2 binds structured RNAs with high affinity, resulting in efficient intramolecular RNA helix disruption. Hexameric σNS oligomerizes into an octamer that binds two RNAs, yet it exhibits only limited RNA-unwinding activity compared to NSP2. Thus, the formation of intersegment RNA-RNA interactions is governed by both helix-unwinding capacity of the chaperones and stability of RNA structure. We propose that this protein-mediated RNA selection mechanism may underpin the high fidelity assembly of multi-segmented RNA genomes in Reoviridae.

Citace poskytuje Crossref.org

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$a To maintain genome integrity, segmented double-stranded RNA viruses of the Reoviridae family must accurately select and package a complete set of up to a dozen distinct genomic RNAs. It is thought that the high fidelity segmented genome assembly involves multiple sequence-specific RNA-RNA interactions between single-stranded RNA segment precursors. These are mediated by virus-encoded non-structural proteins with RNA chaperone-like activities, such as rotavirus (RV) NSP2 and avian reovirus σNS. Here, we compared the abilities of NSP2 and σNS to mediate sequence-specific interactions between RV genomic segment precursors. Despite their similar activities, NSP2 successfully promotes inter-segment association, while σNS fails to do so. To understand the mechanisms underlying such selectivity in promoting inter-molecular duplex formation, we compared RNA-binding and helix-unwinding activities of both proteins. We demonstrate that octameric NSP2 binds structured RNAs with high affinity, resulting in efficient intramolecular RNA helix disruption. Hexameric σNS oligomerizes into an octamer that binds two RNAs, yet it exhibits only limited RNA-unwinding activity compared to NSP2. Thus, the formation of intersegment RNA-RNA interactions is governed by both helix-unwinding capacity of the chaperones and stability of RNA structure. We propose that this protein-mediated RNA selection mechanism may underpin the high fidelity assembly of multi-segmented RNA genomes in Reoviridae.
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$a Borodavka, Alexander $u Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, UK. School of Molecular and Cellular Biology, University of Leeds, Leeds, UK. Department of Chemistry, Center for NanoScience (CeNS), Nanosystems Initiative Munich (NIM) and Centre for Integrated Protein Science Munich (CiPSM), Ludwig Maximilian University of Munich, Munich, Germany.
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$a Barth, Anders $u Department of Chemistry, Center for NanoScience (CeNS), Nanosystems Initiative Munich (NIM) and Centre for Integrated Protein Science Munich (CiPSM), Ludwig Maximilian University of Munich, Munich, Germany.
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$a Calabrese, Antonio N $u Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, UK. School of Molecular and Cellular Biology, University of Leeds, Leeds, UK.
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$a Mojzes, Peter $u Institute of Physics, Faculty of Mathematics and Physics, Charles University, Ke Karlovu 5, CZ-12116 Prague 2, Czech Republic.
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$a Cockburn, Joseph J B $u Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, UK. School of Molecular and Cellular Biology, University of Leeds, Leeds, UK.
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$a Lamb, Don C $u Department of Chemistry, Center for NanoScience (CeNS), Nanosystems Initiative Munich (NIM) and Centre for Integrated Protein Science Munich (CiPSM), Ludwig Maximilian University of Munich, Munich, Germany.
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$a Tuma, Roman $u Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, UK. School of Molecular and Cellular Biology, University of Leeds, Leeds, UK. Faculty of Science, University of South Bohemia, Ceske Budejovice, Czech Republic.
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