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J. Biol. Chem., Vol. 279, Issue 6, 4394-4403, February 6, 2004

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Nucleoside and RNA Triphosphatase Activities of Orthoreovirus Transcriptase Cofactor µ2^*

Jonghwa Kim, John S. L. Parker¶, Kenneth E. Murray, and Max L. Nibert||

From the Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, Massachusetts 02115 and the Department of Biochemistry, University of Wisconsin, Madison, Wisconsin 53706

The mammalian Orthoreovirus (mORV) core particle is an icosahedral multienzyme complex for viral mRNA synthesis and provides a delimited system for mechanistic studies of that process. Previous genetic results have identified the mORV µ 2 protein as a determinant of viral strain differences in the transcriptase and nucleoside triphosphatase activities of cores. New results in this report provided biochemical and genetic evidence that purified µ2 is itself a divalent cation-dependent nucleoside triphosphatase that can remove the 5' -phosphate from RNA as well. Alanine substitutions in a putative nucleotide binding region of µ2 abrogated both functions but did not affect the purification profile of the protein or its known associations with microtubules and mORV µNS protein in vivo. In vitro microtubule binding by purified µ2 was also demonstrated and not affected by the mutations. Purified µ2 was further demonstrated to interact in vitro with the mORV RNA-dependent RNA polymerase, 3, and the presence of 3 mildly stimulated the triphosphatase activities of µ2. These findings confirm that µ2 is an enzymatic component of the mORV core and may contribute several possible functions to viral mRNA synthesis.

Received for publication, August 5, 2003 , and in revised form, October 21, 2003.

^* This work was supported in part by National Institutes of Health Public Health Service Grants R01 AI47904 (to M. L. N.) and K08 AI52209 (to J. S. L. P.) and by a Harvard Foundation-Giovanni Armenise Junior Faculty Research Grant (to M. L. N.). 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.

^¶ Present address: James A. Baker Institute for Animal Health, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853.

^|| To whom correspondence should be addressed: Dept. of Microbiology and Molecular Genetics, 200 Longwood Ave., Boston, MA 02115. Tel.: 617-645-3680; Fax: 617-738-7664; E-mail: mnibert{at}hms.harvard.edu.

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