Phylogenetic analysis of the MCL1 BH3 binding groove and rBH3 sequence motifs in the p53 and INK4 protein families
Fig 3
Phylogenetic tree and conservation of the rBH3 motif in the p53 protein family.
(A) Neighbor-joining phylogenetic tree analyzing 581 sequences of the p53 protein family in jawed vertebrates (151 p53 sequences, 213 p63 sequences, and 217 p73 sequences). Sequences of p53, p63, and p73 are indicated by blue, red, and green branches respectively and the organism class is indicated by colors along the outside of the tree. The domain structure [59] of the protein is displayed around the outside of the tree, and the structure of the tetramerization domain`is shown above that region in the domain structure (PDBS: P53-1AIE [56], p63-3ZY1 [57], p73-2WQI [58]). Abbreviations: TA-Transactivation Domain, PR-Proline Rich Region, DBD-DNA Binding Domain, SAM- Sterile-α Motif, TID-Transactivation Inhibitory Domain. (B) and (C) The p73 and p63 sequences used to construct the phylogenetic tree were aligned using Clustal Omega and the alignment was analyzed for conservation using sequence logos. The residues are colored based on their chemical properties, with polar residues (G, S, T, Y, C, Q, N) colored in green, basic residues (K, R, H) colored in blue, acidic (D, E) colored in red, and hydrophobic residues (A, V, L, I, P, W, F, M) in black. The three residues known to be important for binding (two hydrophobic residues and one acidic residue) are indicated by blue and red asterisks respectively. The rBH3 and surrounding sequence of the tetramerization domain are strongly conserved in the analyzed sequences (p73-217 total sequences, 4 chondrichthyan, 34 osteichthyan, 7 amphibian, 97 avian, 8 reptilian, and 67 mammalian, p63-213 total sequences, 4 chondrichthyan, 46 osteichthyan, 6 amphibian, 70 avian, 8 reptilian, and 79 mammalian).