At-GDI1 from Arabidopsis thaliana encodes a rab-specific GDP dissociation inhibitor that complements the sec19 mutation of Saccharomyces cerevisiae.

Rab GTPases play a central role in the control of vesicular membrane traffic. These proteins cycle between cytosolic and membrane-bound compartments in a guanine nucleotide-dependent manner, a process that is regulated by several accessory proteins. Of particular interest are the Rab guanosine nucleotide diphosphate dissociation inhibitor proteins (Rab-GDI) which bind to prenylated Rab GTPases, slow the rate of GDP dissociation and escort GDP bound Rab proteins to their target membranes and retrieve them after completion of their catalytic cycle. We have cloned from Arabidopsis thaliana a cDNA coding for the Rab guanosine diphosphate dissociation inhibitor (AtGDI1) by functional complementation of the Saccharomyces cerevisiae sec19-1 mutant. The Arabidopsis cDNA potentially encodes a 49850 Da protein which is homologous to yeast GDI (49%) and to other members of the Rab-GDI family (49-63%). Northern blot analysis indicates that the mRNA is expressed in all tissues examined. The existence of a plant homologue of the Rab-GDI family indicates that the basic vesicle traffic control machinery may be highly conserved in plants as it is in yeast and mammals.