title: Leader proteinase of the beet yellows closterovirus: mutation analysis of the function in genome amplification.
abstract: 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.
authors.affiliation: Department of Botany and Plant Pathology, Oregon State University, Corvallis, Oregon 97331, USA.
authors.forename: C W
authors.initials: CW
authors.lastname: Peng
authors.forename: V V
authors.initials: VV
authors.lastname: Dolja
mesh_terms: D017790:Closterovirus / Q000201:enzymology* / Q000235:genetics; D010450:Endopeptidases / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D016679:Genome, Viral; D009154:Mutation; D016366:Open Reading Frames; D012367:RNA, Viral / Q000096:biosynthesis; D013329:Structure-Activity Relationship; D014162:Transfection
chemical_list: D012367:RNA, Viral; D010450:Endopeptidases