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• W2078999710 startingPage "31542" @default.
• W2078999710 abstract "VP55, the vaccinia poly(A) polymerase catalytic subunit, interacts with oligonucleotide primers via two uridylate recognition sites (Deng, L., and Gershon, P. D. (1997) <i>EMBO J.</i> 16, 1103–1113). Here, we show that the cognate RNA sequence comprises a 5′-rU₂-N₁₅-rU-3′ motif (where N=any deoxyribo or ribonucleotide), embedded within oligonucleotide primers 29–30 nucleotides (nt), or greater, in length. Nine residues separate the 3′-most ribouridylate of the optimally positioned motif from the primer 3′-OH. A ribose sugar at the extreme 3′-terminal nucleotide of the primer is absolutely required for VP55's adenylyltransferase activity, but not for stable VP55-RNA interaction. A ribose at position −3 markedly stimulates both adenylyltransferase activity and stable binding. The use of uridine analogs indicated (i) those functional groups of the uracil base which contribute to stable VP55-primer interaction, and (ii) that VP55's ability to discriminate uracil from cytosine stems largely from the requirement for a protonated N3 nitrogen within the pyrimidine ring. The rU₂-N₁₅-rU motif was identified within the uridylate-rich 3′ end of a naturally occurring vaccinia mRNA. However, oligonucleotides whose only internal uridylates comprised the motif supported only a 3–5-nt processive burst of oligo(A) tail addition, as opposed to the ∼30–35-nt burst observed with the naturally occurring 3′ end." @default.
• W2078999710 created "2016-06-24" @default.
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• W2078999710 date "1997-12-01" @default.
• W2078999710 modified "2023-09-30" @default.
• W2078999710 title "Specific Recognition of an rU2-N15-rU Motif by VP55, the Vaccinia Virus Poly(A) Polymerase Catalytic Subunit" @default.
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• W2078999710 doi "https://doi.org/10.1074/jbc.272.50.31542" @default.
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