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Plant Cell, Vol. 12, 343-356, March 2000, Copyright © 2000, American Society of Plant Physiologists

A Conserved Domain of the Arabidopsis GNOM Protein Mediates Subunit Interaction and Cyclophilin 5 Binding

Markus Grebea, José Gadeaa, Thomas Steinmanna, Marika Kientza, Jens-Ulrich Rahfeldb, Klaus Salchertc, Csaba Konczc, and Gerd Jürgensa
a Entwicklungsgenetik, Zentrum für Molekularbiologie der Pflanzen, Universität Tübingen, Auf der Morgenstelle 1, D-72076 Tübingen, Germany
b Forschungsstelle der Max-Planck-Gesellschaft, Enzymologie der Proteinfaltung, D-06120 Halle, Germany
c Max-Planck-Institut für Züchtungsforschung, D-50829 Cologne, Germany

Correspondence to: Gerd Jürgens, gerd.juergens{at}uni-tuebingen.de (E-mail), 49-7071-29-5797 (fax)

The Arabidopsis GNOM protein, a guanine nucleotide exchange factor (GEF) that acts on ADP ribosylation factor (ARF)–type G proteins, is required for coordination of cell polarity along the apical–basal embryo axis. Interallelic complementation of gnom mutants suggested that dimerization is involved in GNOM function. Here, direct interaction between GNOM molecules is demonstrated in vitro and by using a yeast two-hybrid system. Interaction was confined to an N-terminal domain conserved within a subgroup of large ARF GEFs. The same domain mediated in vitro binding to cyclophilin 5 (Cyp5), which was identified as a GNOM interactor in two-hybrid screening. Cyp5 displayed peptidylprolyl cis/trans–isomerase and protein refolding activities that were sensitive to cyclosporin A. Cyp5 protein accumulated in several plant organs and, like GNOM, was partitioned between cytosolic and membrane fractions. Cyp5 protein was also expressed in the developing embryo. Our results suggest that Cyp5 may regulate the ARF GEF function of the GNOM protein during embryogenesis.




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