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THE PLANT CELL, Vol 8, Issue 12 2265-2276, Copyright © 1996 by American Society of Plant Biologists
Cloning of a cDNA Encoding a Plasma Membrane-Associated, Uronide Binding Phosphoprotein with Physical Properties Similar to Viral Movement Proteins
P. Reymond, B. Kunz, K. Paul-Pletzer, R. Grimm, C. Eckerskorn and E. E. Farmer
Institut de Biologie et de Physiologie Vegetales, Batiment de Biologie, Universite de Lausanne, 1015 Lausanne, Switzerland
Oligogalacturonides are structural and regulatory homopolymers from the
extracellular pectic matrix of plants. In vitro micromolar concentrations
of oligogalacturonates and polygalacturonates were shown previously to
stimulate the phosphorylation of a small plasma membrane-associated protein
in potato. Immunologically cross-reactive proteins were detected in plasma
membrane-enriched fractions from all angiosperm subclasses in the Cronquist
system. Polygalacturonate-enhanced phosphorylation of the protein was
observed in four of the six dicotyledon subclasses but not in any of the
five monocotyledon subclasses. A cDNA for the protein was cloned from
potato. The deduced protein is extremely hydrophilic and has a proline-rich
N terminus. The C-terminal half of the protein was predicted to be a coiled
coil, suggesting that the protein interacts with other macromolecules. The
recombinant protein was found to bind both simple and complex
galacturonides. The behavior of the protein suggests several parallels with
viral proteins involved in intercellular communication.
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