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Fig. 1. The co-chaperone TPR1 binds to HSP90 and VAP-33. (A) Representation of the HSP90, TPR1 and VAP-33 constructs used for the two-hybrid experiments. The top row shows, from left to right, full-length TPR1, Tpr1unique and the fragment containing the TPR domain. The column on the left shows, from top to bottom, Hsp90C, full-length VAP-33, VAP-33 lacking its membrane anchor tail, the MSP domain of VAP-33 and the fragment containing the coiled-coil region (represented by blue double-tilde). The plus (+) and minus (–) symbols indicate the presence or absence of an interaction when various constructs were co-transformed in yeast cells and tested for growth as shown in panel B. (B) Constructs in the pAS2-1 vector were co-transformed with pACT2 constructs into S. cerevisiae Y190 as indicated, with empty vectors serving as a control. After growth on SD/–Trp, –Leu plates, cells were re-plated on the same medium to confirm the presence of the pAS2-1 and pACT vectors (left panel) and on SD/–Trp, –Leu, –His plates containing 25 mM 3-amino-1,2,4-triazole (right panel) to select for protein interactions. TPR1 and Tpr1TPR interacted with Hsp90C, whereas TPR1 and Tpr1unique interacted with VAP-33, VAP-33(–tail) and VAP-33MSP. (C) Illustration of the complex comprising HSP90, TPR1 and the membrane-anchored protein VAP-33 based on our yeast two-hybrid data.
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