Inproceedings: An article in a conference proceedings.
Poster: Summary – with images – on one page of the results of a researche project. The summaries of the poster must be entered in "Abstract" and not "Poster".
Remorin, a uronide binding protein with physical properties similar to the tobacco mosaic virus movement protein
Title of the conference
Plant Biology '97, Annual Meetings of the American Society of Plant Physiologists and the Canadian Society of Plant Physiologists with the invited participation of the Japanese Society of Plant Physiologists and the Australian Society of Plant Physiologists
Vancouver, Canada, August 2-8, 1997
The extracellular pectic matrix is a rich source of oligogalacturonic acid (OGA), one of the most abundant polymeric regulatory molecules on the earth's surface. OGAs regulate the expression of a variety of defense genes and have also been implicated in developmental processes. Little is known about how cells perceive OGAs and we have been attempting to characterise proteins capable of interacting with these molecules. We recently succeeded in cloning a cDNA encoding a small OGA-binding protein, remorin. OGA-binding to remorin is not highly specific, the protein binds homogalacturonides, complex pectic polymers and the animal polyuronide heparin. This lack of specificity contrasts with that often observed with classical receptors and the function of remorin remains to be discovered. Remorin copurifies with the plasma membrane but is a very hydrophilic polypeptide. Its behavior during cell fractionation, as well as a number of properties including the OGA-stimulated in vitro phosphorylation and preliminary localization studies, all suggest parallels with some viral movement proteins. Some of these comparisons will be presented. Experiments to directly test for the possible role of this protein in cell-to-cell signalling are in progress. EEF is supported by FNRS grant 31-3672-92.
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