PMID: 9532800Apr 9, 1998Paper

Detection of potato virus Y P1 protein in infected cells and analysis of its cleavage site

Bioscience, Biotechnology, and Biochemistry
L J YangT Uozumi

Abstract

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.

Citations

Feb 28, 2001·Virus Research·S Urcuqui-InchimaF Bernardi
Sep 23, 2008·Biochemical Genetics·Satendra K MangrauthiaShelly Praveen
Jul 27, 2010·Molecular Plant-microbe Interactions : MPMI·Kenji S NakaharaIchiro Uyeda
Jul 1, 2005·Molecular Plant Pathology·Michael J AdamsFrederic Beaudoin

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