Table 1.

Interaction of the PDZ domains of ZO-1 and ZO-2 with a construct encoding the C-terminal region of ARVCF (amino acids 670-893) or a mutant thereof (ARVCFΔP) in which the SWV amino acids encoding a putative PDZ-binding motif were changed to alanines

	ARVCF	ARVCF(ΔP)	Cx-45	Library vector	Laminin	T-Ag
ZO-1 PDZ	+++	-	+++	-	-	nd
ZO-2 PDZ	+++	-	-	-	-	nd
ZO-3 PDZ	-	-	+++	-	-	nd
Bait vector	-	-	-	-	-	-
p53	-	-	-	-	-	+++

Interactions were determined by monitoring growth of cotransformed yeast on selective media and β-galactosidase activity. Similar results were obtained under low and high stringency conditions. Empty bait (pGBKT7) and library (pACT2) plasmids and a lamin construct served as negative controls. T-antigen (T-Ag) and p53, two known interaction partners, were used as a positive control. Growth on dropout media and β-galactosidase activities for yeast coexpressing T-Ag and p53 (positive control) were similar for clones coexpressing the C-terminus of ARVCF and the PDZ-domains of ZO-1 and ZO-2. Since the ZO-3 bait can interact with the PDZ-motif in Cx-45, the lack of an interaction with ARVCF was not due to the experimental set up. +++, interaction; -, no interaction; nd, not determined.