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Journal of Virology, October 2000, p. 9766-9770, Vol. 74, No. 20
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Leader Proteinase of the Beet Yellows Closterovirus: Mutation Analysis of the Function in Genome Amplification

Chih-Wen Peng1 and Valerian V. Dolja1,2,*

Department of Botany and Plant Pathology1 and Center for Gene Research and Biotechnology,2 Oregon State University, Corvallis, Oregon 97331

Received 9 March 2000/Accepted 19 July 2000

The beet yellows closterovirus leader proteinase (L-Pro) possesses a C-terminal proteinase domain and a nonproteolytic N-terminal domain. It was found that although L-Pro is not essential for basal-level replication, deletion of its N-terminal domain resulted in a 1,000-fold reduction in RNA accumulation. Mutagenic analysis of the N-terminal domain revealed its structural flexibility except for the 54-codon-long, 5'-terminal element in the corresponding open reading frame that is critical for efficient RNA amplification at both RNA and protein levels.

* Corresponding author. Mailing address: Department of Botany and Plant Pathology, Oregon State University, Cordley Hall 2082, Corvallis, OR 97330. Phone: (541) 737-5472. Fax: (541) 737-3573. E-mail: doljav{at}bcc.orst.edu.

Journal of Virology, October 2000, p. 9766-9770, Vol. 74, No. 20
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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