Methylation of reovirus oligonucleotides in Vivo and in Vitro

C. A. Carter

doi:10.1016/S0042-6822(77)80002-0

Methylation of reovirus oligonucleotides in Vivo and in Vitro

C. A. Carter

Microbiology and Immunology

Research output: Contribution to journal › Article › peer-review

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Abstract

Reovirus-associated methylases, located in the viral core, function independently of RNA polymerase and guanylyl transferase to modify the 5′-termini of single-stranded oligonucleotides present in the virion. A previously undiscovered class of oligomers, 5′-terminated by GpppG, serve as substrate and are converted to m⁷GpppGp(Xp)n and m⁷GpppG^mp(Xp)n by addition of methyl groups from S-adenosyl methionine. This reaction occurs under conditions distinct from those stimulating mRNA methylation.

Original language	English
Pages (from-to)	249-259
Number of pages	11
Journal	Virology
Volume	80
Issue number	2
DOIs	https://doi.org/10.1016/S0042-6822(77)80002-0
State	Published - Jul 15 1977

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title = "Methylation of reovirus oligonucleotides in Vivo and in Vitro",

abstract = "Reovirus-associated methylases, located in the viral core, function independently of RNA polymerase and guanylyl transferase to modify the 5′-termini of single-stranded oligonucleotides present in the virion. A previously undiscovered class of oligomers, 5′-terminated by GpppG, serve as substrate and are converted to m7GpppGp(Xp)n and m7GpppGmp(Xp)n by addition of methyl groups from S-adenosyl methionine. This reaction occurs under conditions distinct from those stimulating mRNA methylation.",

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T1 - Methylation of reovirus oligonucleotides in Vivo and in Vitro

AU - Carter, C. A.

PY - 1977/7/15

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N2 - Reovirus-associated methylases, located in the viral core, function independently of RNA polymerase and guanylyl transferase to modify the 5′-termini of single-stranded oligonucleotides present in the virion. A previously undiscovered class of oligomers, 5′-terminated by GpppG, serve as substrate and are converted to m7GpppGp(Xp)n and m7GpppGmp(Xp)n by addition of methyl groups from S-adenosyl methionine. This reaction occurs under conditions distinct from those stimulating mRNA methylation.

AB - Reovirus-associated methylases, located in the viral core, function independently of RNA polymerase and guanylyl transferase to modify the 5′-termini of single-stranded oligonucleotides present in the virion. A previously undiscovered class of oligomers, 5′-terminated by GpppG, serve as substrate and are converted to m7GpppGp(Xp)n and m7GpppGmp(Xp)n by addition of methyl groups from S-adenosyl methionine. This reaction occurs under conditions distinct from those stimulating mRNA methylation.

UR - https://www.scopus.com/pages/publications/0017735992

U2 - 10.1016/S0042-6822(77)80002-0

DO - 10.1016/S0042-6822(77)80002-0

M3 - Article

C2 - 888347

AN - SCOPUS:0017735992

SN - 0042-6822

VL - 80

SP - 249

EP - 259

JO - Virology

JF - Virology

IS - 2

ER -

Methylation of reovirus oligonucleotides in Vivo and in Vitro

Abstract

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