Nucleic Acids Research, Vol 27, Issue 2 421-425, Copyright © 1999 by Oxford University Press
D Prufer, L Kawchuk, M Monecke2, S Nowok, R Fischer and W Rohde
Mono- and polyclonal antibodies directed against different domains of the
potato leafroll luteovirus (PLRV) P1 (ORF1) protein were applied to the
analysis of P1 expression during PLRV replication in planta. Western
analyses detected P1 and a protein of approximately 25 kDa (P1- C25) that
accumulated to readily detectable amounts in PLRV-infected plants, but was
not detected by in vitro cell-free translation of P1. P1-C25 represents the
C-terminus of P1 and is a proteolytic cleavage product produced during P1
processing. On the basis of its molecular weight, the N-terminus of P1-C25
is either identical to or located adjacent to the previously identified
PLRV genome-linked protein, VPg. P1-C25 is not associated with virus
particles, and subcellular localization experiments detected P1-C25, but
not P1, in the membrane and cytoplasmic fractions of PLRV-infected cells.
In addition, P1-C25 exhibits nucleic acid-binding properties. On the basis
of its biosynthesis, localization and biochemical properties, P1-C25 may
facilitate the formation of P1/PLRV RNA complexes in which the spatial
proximity allows for covalent bond formation between PLRV RNA and VPg.
ARTICLES
Immunological analysis of potato leafroll luteovirus (PLRV) P1 expression identifies a 25 kDa RNA-binding protein derived via P1 processing
Max-Planck-Institut fur Zuchtungsforschung, Carl-von-Linne Weg 10, 50829 Koln, Germany. pruefer@mpiz-koeln.mpg.de
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