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RdRp or RT, That is the Question

The RNA-dependent RNA polymerase (RdRp) of all known double-stranded RNA viruses is located within the viral particle and is responsible for the transcription and replication of the viral genome. Through an RT-PCR assay, we determined that purified virions, in vitro translated RdRp proteins, and pur...

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Autores principales: Peyambari, Mahtab, Guan, Shengxi, Roossinck, Marilyn J
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8557412/
https://www.ncbi.nlm.nih.gov/pubmed/34352104
http://dx.doi.org/10.1093/molbev/msab235
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author Peyambari, Mahtab
Guan, Shengxi
Roossinck, Marilyn J
author_facet Peyambari, Mahtab
Guan, Shengxi
Roossinck, Marilyn J
author_sort Peyambari, Mahtab
collection PubMed
description The RNA-dependent RNA polymerase (RdRp) of all known double-stranded RNA viruses is located within the viral particle and is responsible for the transcription and replication of the viral genome. Through an RT-PCR assay, we determined that purified virions, in vitro translated RdRp proteins, and purified recombinant RdRp proteins of partitiviruses also have reverse transcriptase (RT) function. We show that partitivirus RdRps 1) synthesized DNA from homologous and heterologous dsRNA templates; 2) are active using both ssRNA and dsRNA templates; and 3) are active at lower temperatures compared to an optimal reaction temperature of commercial RT enzymes. This finding poses an intriguing question: why do partitiviruses, with dsRNA genomes, have a polymerase with RT functions? In comparison, 3Dpol, the RdRp of poliovirus, did not show any RT activity. Our findings lead us to propose a new evolutionary model for RNA viruses where the RdRp of dsRNA viruses could be the ancestor of RdRps.
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spelling pubmed-85574122021-11-01 RdRp or RT, That is the Question Peyambari, Mahtab Guan, Shengxi Roossinck, Marilyn J Mol Biol Evol Discoveries The RNA-dependent RNA polymerase (RdRp) of all known double-stranded RNA viruses is located within the viral particle and is responsible for the transcription and replication of the viral genome. Through an RT-PCR assay, we determined that purified virions, in vitro translated RdRp proteins, and purified recombinant RdRp proteins of partitiviruses also have reverse transcriptase (RT) function. We show that partitivirus RdRps 1) synthesized DNA from homologous and heterologous dsRNA templates; 2) are active using both ssRNA and dsRNA templates; and 3) are active at lower temperatures compared to an optimal reaction temperature of commercial RT enzymes. This finding poses an intriguing question: why do partitiviruses, with dsRNA genomes, have a polymerase with RT functions? In comparison, 3Dpol, the RdRp of poliovirus, did not show any RT activity. Our findings lead us to propose a new evolutionary model for RNA viruses where the RdRp of dsRNA viruses could be the ancestor of RdRps. Oxford University Press 2021-08-05 /pmc/articles/PMC8557412/ /pubmed/34352104 http://dx.doi.org/10.1093/molbev/msab235 Text en © The Author(s) 2021. Published by Oxford University Press on behalf of the Society for Molecular Biology and Evolution. https://creativecommons.org/licenses/by-nc/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial License (https://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com
spellingShingle Discoveries
Peyambari, Mahtab
Guan, Shengxi
Roossinck, Marilyn J
RdRp or RT, That is the Question
title RdRp or RT, That is the Question
title_full RdRp or RT, That is the Question
title_fullStr RdRp or RT, That is the Question
title_full_unstemmed RdRp or RT, That is the Question
title_short RdRp or RT, That is the Question
title_sort rdrp or rt, that is the question
topic Discoveries
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8557412/
https://www.ncbi.nlm.nih.gov/pubmed/34352104
http://dx.doi.org/10.1093/molbev/msab235
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