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• W2046702511 abstract "Expression of reovirus-associated enzymes was detected in purified virions. As reported previously for chymotrypsin-derived viral cores, untreated virions catalyzed the synthesis of short oligonucleotides corresponding to the 5′-terminal sequence of viral mRNAS. Oligonucleotide synthesis by both kinds of particles required a divalent cation, and Mn+2 was more effective than Mg+2. The transcriptase activity in virions, in contrast to viral cores, was apparently incapable of elongating nascent chains. Consequently, virions produced no viral mRNAs during incubation in vitro for several hours. Transcriptase activity as measured by oligonucleotide synthesis was highly temperature dependent in virions and cores (∼51° optimum) and similar to mRNA synthesis by cores. The several other reovirus-associated enzymes involved in 5′-terminal cap formation were also active in virions. They include nucleotide phosphohydrolase, guanylyltransferase and methyltransferase activities. The results indicate that elongation, but not initiation-related transcription events, is prevented in reovirions by structural constraints on the transcriptase/template RNA complex." @default.
• W2046702511 created "2016-06-24" @default.
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• W2046702511 date "1982-04-01" @default.
• W2046702511 modified "2023-09-25" @default.
• W2046702511 title "Reovirus transcriptase and capping enzymes are active in intact virions" @default.
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• W2046702511 doi "https://doi.org/10.1016/0042-6822(82)90329-4" @default.
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