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Journal of Virology, April 2009, p. 3549-3555, Vol. 83, No. 8
0022-538X/09/$08.00+0     doi:10.1128/JVI.02411-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Functional Replacement of a Domain in the Rubella Virus P150 Replicase Protein by the Virus Capsid Protein{triangledown}

Wen-Pin Tzeng and Teryl K. Frey*

Department of Biology, Georgia State University, Atlanta, Georgia 30303

Received 21 November 2008/ Accepted 21 January 2009

The rubella virus (RUBV) capsid (C) protein rescues mutants with a lethal deletion between two in-frame NotI sites in the P150 replicase gene, a deletion encompassing nucleotides 1685 to 2192 of the RUBV genome and amino acids (aa) 548 to 717 of P150 (which has a total length of 1,301 aa). The complete domain rescuable by the C protein was mapped to aa 497 to 803 of P150. Introduction of aa 1 to 277 of the C protein (lacking the C-terminal E2 signal sequence) between the NotI sites in the P150 gene in a replicon construct yielded a viable construct that synthesized viral RNA with wild-type kinetics, indicating that C and this region of P150 share a common function. Further genetic analysis revealed that an arginine-rich motif between aa 60 and 68 of the C protein was necessary for the rescue of {Delta}NotI deletion mutants and substituted for an arginine-rich motif between aa 731 and 735 of the P150 protein when the C protein was introduced into P150. Possible common functions shared by these arginine-rich motifs include RNA binding and interaction with cell proteins.

* Corresponding author. Mailing address: Georgia State University, Biology Department, P.O. Box 4010, Atlanta, GA 30302-4010. Phone: (404) 413-5392. Fax: (404) 413-5301. E-mail: tfrey{at}gsu.edu

{triangledown} Published ahead of print on 28 January 2009.

Journal of Virology, April 2009, p. 3549-3555, Vol. 83, No. 8
0022-538X/09/$08.00+0     doi:10.1128/JVI.02411-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





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