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THE PLANT CELL, Vol 6, Issue 11 1681-1692, Copyright © 1994 by American Society of Plant Biologists
A Fusicoccin Binding Protein Belongs to the Family of 14-3-3 Brain Protein Homologs
HAAJ. Korthout and A. H. de Boer
Department of Plant Physiology and Biochemistry, Institute of Molecular Biological Sciences, Vrije Universiteit, De Boelelaan 1087, 1081 HV Amsterdam, The Netherlands
The fusicoccin binding protein (FCBP) is a highly conserved plasma membrane
protein present in all higher plants tested thus far. It exhibits high- and
low-affinity binding for the fungal toxin fusicoccin (FC). We purified the
active FCBP from a fraction highly enriched in plasma membrane by selective
precipitation and anion exchange chromatography. After SDS-PAGE, the two
FCBP subunits of 30 and 31 kD were detected as major bands. Amino acid
sequence analysis of the 31-kD polypeptide displayed a high degree of
identity with so-called 14-3-3 proteins, a class of mammalian brain
proteins initially described as regulators of neurotransmitter synthesis
and protein kinase C inhibitors. Thereafter, we affinity purified the 30-
and 31-kD FCBP subunits, using biotinylated FC in combination with a
monomeric avidin column. Immunodecoration of these 30- and 31-kD FCBP
subunits with polyclonal antibodies raised against a 14-3-3 homolog from
yeast confirmed the identity of the FCBP as a 14-3-3 homolog. Similar to
all 14-3-3 protein homologs, the FCBP seems to exist as a dimer in native
form. Thus far, the FCBP is the only 14-3-3 homolog with a receptor-like
function. The conserved structure of the 14-3-3 protein family is a further
indication that the FCBP plays an important role in the physiology of
higher plants.
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