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. 2019 May 28;6(6):267–285. doi: 10.15698/mic2019.06.679

Figure 1. FIGURE 1: Structural features of the Yap family DNA binding domain.

Figure 1

The sequences of the eight Yap DNA binding domains (i.e. the basic region of the bZIP motif) are compared with the equivalent region of Gcn4, the classical yeast AP-1 factor, used as an outgroup. A green background highlights the positions, whose physico-chemical properties are conserved in the Yap family. The most conserved residues are in bold. The Yap8 specific residues are in blue. The Yap1 amino-acids which were predicted to contact DNA based on structural studies [12, 140] have been underlined by a black box. The Gcn4 residues involved in DNA interaction are highlighted by pink boxes. The rooted tree and the multiple alignment were obtained from ClustalW (https://www.genome.jp/tools-bin/clustalw), using the bZIP sequences and the 100 flanking amino-acids.