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Fig. 6. Mapping of the KIF13B binding site within centaurin-{alpha}1 using yeast two-hybrid analysis. (A) Schematic representation of the domain structure (GAP domain, aa 1-126; N-PH, aa 130-230; C-PH, aa 253-356) and various deletion mutants of centaurin-{alpha}1. (B) Interaction of KIF13B with the full-length (FL) and deletion constructs of centaurin-{alpha}1. The full-length and deletion mutants of centaurin-{alpha}1 fused to the DNA binding domain of LexA (bait) pBTM, were co-transformed with KIF13B{Delta} fused to the activation domain of Gal4 (prey) into the L40 yeast strain, and the transformants analysed for their ability to grow on medium lacking histidine, and to metabolise X-gal by ß-galactosidase. Panels, left to right, show three clones of each transformant grown on medium with (+H) and without (–H) histidine, and the filter ß-galactosidase assay (ß-gal). The experiment was performed three times with three different yeast transformations with identical results.





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