Detection of potato virus Y P1 protein in infected cells and analysis of its cleavage site.
The P1 protein is liberated from the N-terminal region of the potyviral polyprotein by cleavage depending on its own autoproteolytic activity. Existence of the 32-kDa P1 protein in tobacco plants infected with potato virus Y ordinary strain (PVY-O) was detected by an antiserum against a recombinant PVY-O P1 protein. In vivo analysis using tobacco protoplasts confirmed that the Phe284-Ser285 was the cleavage site separating the P1 protein from the PVY-O polyprotein. Phe284 was indispensable for proteolysis and Ser285 was needed for optimal cleavage susceptibility.
Yang
L J
LJ
Department of Biotechnology, Graduate School of Agricultural and Life Sciences, University of Tokyo, Japan.
Hidaka
M
M
Masaki
H
H
Uozumi
T
T
D000595:Amino Acid Sequence; D015153:Blotting, Western; D004591:Electrophoresis, Polyacrylamide Gel; D008969:Molecular Sequence Data; D010447:Peptide Hydrolases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D010947:Plants, Toxic; D010957:Plasmids; D017800:Potyvirus / Q000737:chemistry* / Q000235:genetics / Q000276:immunology; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D016415:Sequence Alignment; D014026:Nicotiana / Q000821:virology; D014764:Viral Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification
D011994:Recombinant Proteins; D014764:Viral Proteins; D010447:Peptide Hydrolases