Sequencing, genomic localization and initial characterization of the VPg of pea enation mosaic enamovirus.
The amino acid sequence of the genome-linked viral protein (VPg) of pea enation mosaic enamovirus (PEMV) has been determined. The VPg is encoded by nt 1811-1894 within ORF1 of RNA1 downstream of the proteinase motif. Direct N terminus sequencing of intact and endoproteinase Asp-N-digested VPg combined with electrospray mass spectroscopy confirmed that the VPg is composed of 28 amino acids with a molecular mass of 3138 Da. The context of the N and C terminus residues as well as the position and size of the VPg suggest that the mature VPg may be generated via post-translational proteolytic processing of the polyprotein arrangement of membrane anchor-proteinase-VPg-polymerase encoded by ORFs 1 and 2. Computer comparisons did not reveal any significant similarity between the VPg of PEMV and any other sequences including those of the VPgs of related subgroup II luteoviruses.
Wobus
C E
CE
Department of Botany and Plant Pathology, Michigan State University, East Lansing 48824, USA.
Skaf
J S
JS
Schultz
M H
MH
de Zoeten
G A
GA
D000595:Amino Acid Sequence; D002874:Chromosome Mapping; D017793:Luteovirus / Q000235:genetics*; D008969:Molecular Sequence Data; D018532:Pisum sativum / Q000821:virology; D014758:Viral Core Proteins / Q000235:genetics*
D014758:Viral Core Proteins