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J Biol Chem, Vol. 275, Issue 20, 15520-15525, May 19, 2000
From the Laboratory of Bioactive Natural Products Chemistry,
Graduate School of Bio-agricultural Sciences, Nagoya University,
Chikusa, Nagoya 464-8601, Japan
Plant cells in culture secrete a sulfated peptide
named phytosulfokine-
120- and 160-kDa Receptors for Endogenous Mitogenic Peptide,
Phytosulfokine-
, in Rice Plasma Membranes*
and
(PSK-), and this peptide induces the cell
division and/or cell differentiation by means of specific high and low affinity receptors. Putative receptor proteins for this autocrine type
growth factor were identified by photoaffinity labeling of plasma
membrane fractions derived from rice suspension cells. Incubation of
membranes with a photoactivable 125I-labeled PSK-
analog,
[N
-(4-azidosalicyl)Lys5]PSK-
(AS-PSK-), followed by UV irradiation resulted in specific labeling
of 120- and 160-kDa bands in SDS-polyacrylamide gel electrophoresis. The labeling of both bands was completely inhibited by unlabeled PSK- and partially decreased by PSK- analogs possessing moderate binding activities. In contrast, PSK- analogs that have no
biological activity showed no competition for
125I-AS-PSK- binding, confirming the specificity of
binding proteins. Analysis of the affinity of 125I
incorporation into the protein by ligand saturation experiments gave
apparent Kd values of 5.0 nM for the
120-kDa band and 5.4 nM for the 160-kDa band, suggesting
that both proteins correspond to the high affinity binding site.
Treatment of 125I-AS-PSK- cross-linked proteins with
peptide N-glycosidase F demonstrated that both proteins
contained approximately 10 kDa of N-linked
oligosaccharides. Specific cross-linking of 125I-AS-PSK-
was also observed by using plasma membranes derived from carrot and
tobacco cells, indicating the widespread occurrence of the binding
proteins. Together, these data suggest that the 120- and 160-kDa
proteins are PSK- receptors that mediate the biological activities
of PSK-.
*
This work was supported by the Program for Promotion of
Basic Research Activities for Innovative Biosciences.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence and reprint requests should be addressed.
Tel.: 81-52-789-5552; Fax: +81-52-789-4118; E-mail:
matsu@agr.nagoya-u.ac.jp.
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