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• W1270603338 abstract "This chapter discusses that blocked and methylated 5'-termini of reovirus mRNA are formed by viral cores at an early stage of transcription. Cores incubated in a complete transcription reaction mixture for 30 seconds synthesize the “cap” structure, m7GpppGm-C. The dinucleotide ppG-C functions as substrate for a core-associated guanylyltransferase and is converted to GpppG-C by addition of pG from pppG( GTP). For optimal conversion both the diphosphate terminus and phosphodiester bond are required. pG-C is not a substrate, but pppG-C is utilized after removal of the γ-phosphate by a core nucleotide phosphohydrolase. Methyltransferases, also present in cores, transfer methyl groups sequentially from S-adenosylmethionine to the 7-position of the 5'-terminal G of GpppG-C and to the 2'-OH of the penultimate G. The chapter reviews that GpppG-C is hydrolyzed by cores in the presence of pyrophosphate to ppG-C, the predominant 5'-terminal structure of reovirus mRNA made in the absence of S-adenosylmethionine. 7-Methylation prevents pyrophosphorolysis of m7GpppG-C, which may explain the increased proportion of blocked, methylated 5' termini in viral mRNA synthesized in the presence of S-adenosylmethionine. On the basis of these findings, it proposes a series of reactions for the synthesis of reovirus mRNA caps, and some characteristic features of the enzymes involved in these reactions are also discussed." @default.
• W1270603338 created "2016-06-24" @default.
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• W1270603338 date "1977-01-01" @default.
• W1270603338 modified "2023-10-16" @default.
• W1270603338 title "Caps in Eukaryotic mRNAs: Mechanism of Formation of Reovirus mRNA 5′-Terminal m7GpppGm-C" @default.
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• W1270603338 doi "https://doi.org/10.1016/s0079-6603(08)60905-8" @default.
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