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J. Biol. Chem., Vol. 279, Issue 37, 38103-38110, September 10, 2004

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Uridylylation of the Potyvirus VPg by Viral Replicase NIb Correlates with the Nucleotide Binding Capacity of VPg^*

Pietri Puustinen and Kristiina Mäkinen

From the Department of Applied Biology, P. O. Box 27, University of Helsinki, Helsinki 00014, Finland

Poty- and picornaviruses share similar genome organizations and polyprotein processing strategies. By analogy to picornaviruses it has been proposed that the genome-linked protein VPg may serve as a primer for genome replication of potyviruses. The multifunctional VPg of potato virus A (PVA; genus Potyvirus) was found to be uridylylated by NIb, the RNA polymerase of PVA. The nucleotidylation activity of NIb is more efficient in the presence of Mn²⁺ than Mg²⁺ and does not require an RNA template. Our results suggest that the nucleotidylation reaction exhibits weak preference for UTP over the other NTPs. An NTP-binding experiment with oxidized [-³²P]UTP revealed that PVA VPg contains an NTP-binding site. Deletion of a 7-amino acid-long putative NTP-binding site from VPg reduced nucleotide-binding capacity and debilitated uridylylation reaction. These results provide evidence that VPg may play a similar role in RNA synthesis of potyviruses as it does in the case of picornaviruses.

Received for publication, March 16, 2004 , and in revised form, June 24, 2004.

^* This work was supported in part by Grants 53862 and 206870 from the Academy of Finland. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed. Tel.: 358-9-29258342; Fax: 358-9-19158633; E-mail: kristiina.makinen{at}helsinki.fi.

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