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Plant Physiol, August 2001, Vol. 126, pp. 1480-1492
Isolation and Characterization of Kinase Interacting Protein 1, a
Pollen Protein That Interacts with the Kinase Domain of PRK1, a
Receptor-Like Kinase of Petunia1
Andrea L.
Skirpan,
Andrew G.
McCubbin,
Takeshi
Ishimizu,
Xi
Wang,
Yi
Hu,
Peter E.
Dowd,
Hong
Ma, and
Teh-hui
Kao*
Departments of Biochemistry and Molecular Biology (A.L.S., A.G.M.,
X.W., P.E.D., T.-h.K.) and Biology and the Life Sciences Consortium
(Y.H., H.M.) and Intercollege Graduate Degree Program in Plant
Physiology (H.M., T.-h.K.), The Pennsylvania State University,
University Park, Pennsylvania 16802; and Graduate School of Science,
Osaka University, 1-1 Machikaneyama-cho, Toyonaka 560-0043, Japan
(T.I.)
Many receptor-like kinases have been identified in plants and have
been shown by genetic or transgenic knockouts to play diverse physiological roles; however, to date, the cytosolic interacting proteins of relatively few of these kinases have been identified. We
have previously identified a predominantly pollen-expressed receptor-like kinase of petunia (Petunia inflata), named
PRK1, and we have shown by the antisense RNA approach that it is
required for microspores to progress from the unicellular to bicellular stage. To investigate the PRK1-mediated signal transduction pathway, PRK1-K cDNA, encoding most of the cytoplasmic domain of
PRK1, was used as bait in yeast (Saccharomyces
cerevisiae) two-hybrid screens of pollen/pollen tube cDNA
libraries of petunia. A protein named kinase interacting protein 1 (KIP1) was found to interact very strongly with PRK1-K. This
interaction was greatly reduced when lysine-462 of PRK1-K, believed to
be essential for kinase activity, was replaced with arginine (the
resulting protein is named PRK1-K462R). The amino acid sequence of KIP1
deduced from full-length cDNA contains an EF-hand
Ca2+-binding motif and nine predicted coiled-coil regions.
The yeast two-hybrid assay and affinity chromatography showed that
KIP1 interacts with itself to form a dimer or higher multimer.
KIP1 is present in a single copy in the genome, and is
expressed predominantly in pollen with a similar temporal pattern to
PRK1. In situ hybridization showed that
PRK1 and KIP1 transcripts were localized
in the cytoplasm of pollen. PRK1-K phosphorylated KIP1-NT (amino acids
1-716), whereas PRK1-K462R only weakly phosphorylated KIP1-NT in
vitro.
1
This work was supported by the U.S. Department
of Agriculture (grant nos. 96-35304-3635 and 99-35304-8004 to
T.-h.K.), by the National Science Foundation (grant nos. MCB-9728772
and IBN-0077832), by the Biology Department and the Life Sciences
Consortium of The Pennsylvania State University (to H.M.), by a
pre-doctoral Fellowship for Students with Disabilities from the
National Institutes of Health (to P.E.D.), and by a Research Fellowship
for Young Scientists from the Japan Society for the Promotion of
Science (to T.I.).
*
Corresponding author; e-mail txk3{at}psu.edu; fax
814-863-9416.
© 2001 American Society of Plant Physiologists
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