RdRp or RT, That is the Question

• Published in: Molecular biology and evolution Vol. 38; no. 11; pp. 5082 - 5091
• Main Authors: Peyambari, Mahtab, Guan, Shengxi, Roossinck, Marilyn J
• Format: Journal Article
• Language: English
• Published: United States Oxford University Press 01.11.2021
• Subjects: Analysis; Discoveries; DNA; DNA polymerases; Enzymes; Ethylenediaminetetraacetic acid; Evolution; Genetic transcription; Genome, Viral; Genomics; RNA; RNA Viruses - genetics; RNA, Double-Stranded - genetics; RNA, Viral - genetics; RNA-Dependent RNA Polymerase - genetics; RNA-Directed DNA Polymerase - genetics; partitivirus; reverse transcriptase; polymerase origins; RNA-dependent RNA polymerase; virus evolution
• ISSN: 0737-4038; 1537-1719
• DOI: 10.1093/molbev/msab235

Abstract 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.