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PMID: 6246277 Published · ppublish English Journal Article

mRNA capping enzymes are masked in reovirus progeny subviral particles.

Journal of virology ·Vol. 34 ·No. 2 ·1980-05-00 ·Pages 490-6

Skup D, Millward S

Abstract

We examined the enzyme activities associated with progeny subviral particles isolated from L-cells infected with reovirus at 12 h postinfection. Activities normally present in reovirus cores were also found to be present in the progeny subviral particles, with the exception of the capping enzymes. The methylase and guanyl transferase activities, which constitute the capping system, were present in a masked form that could be activated by chymotrypsin digestion. The appearance of these progeny subviral particles in infected cells coincided with the time when mRNA synthesis was maximal, suggesting that viral mRNA synthesized at later times is uncapped.

MeSH Terms
Adenosine Triphosphatases/metabolism Chymotrypsin/pharmacology DNA-Directed RNA Polymerases/metabolism Diphosphates/metabolism Kinetics Mammalian orthoreovirus 3/enzymology,growth & development RNA, Messenger/metabolism RNA, Viral/metabolism Reoviridae/enzymology Virion/enzymology tRNA Methyltransferases/metabolism
Chemicals
Diphosphates RNA, Messenger RNA, Viral tRNA Methyltransferases DNA-Directed RNA Polymerases Chymotrypsin Adenosine Triphosphatases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Skup D
Millward S
References (23)
23 references, click to expand
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Article Info
Journal
Journal of virology
Abbr.
J Virol
ISSN
0022-538X
DOI
10.1128/JVI.34.2.490-496.1980
Published
1980-05-00
Pages
490-6
Language
English
Region
United States
NLM ID
0113724
PMCID
PMC288728
Subset
IM
External Links
PubMed source DOI: 10.1128/JVI.34.2.490-496.1980 PMC Full Text View journal details
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