Phylogeny of <i>Mlxip</i> and <i>Mlxipl</i> coding sequences.

<p>Phylogeny inferred by the Bayesian method, implemented in MrBayes version 3.2.2, is shown, using the coding sequence alignment from <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0149682#pone.0149682.s002" target="_blank">S2 Fig</a> based on the alignment presented in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0149682#pone.0149682.s012" target="_blank">S12 Fig</a>. The phylogeny is rooted between the sequences for <i>Mlxip</i> (shown in the upper portion) and <i>Mlxipl</i> (lower portion). Branch lengths are proportional to the number of inferred nucleotide substitutions. Numbers at the node represent posterior probabilities after 2,000,000 generations. Similar phylogenies were generated when Maximum likelihood or neighbor-joining methods were used.</p

Introns in <i>Mlxip</i> and <i>Mlxipl</i> genes are at homologous locations.

<p>Alignment of human and mouse ChREBP, MondoA, and Mlx (encoded by <i>MLXIPL</i>, <i>MLXIP</i>, and <i>MLX</i>, respectively) protein sequences and <i>Drosophila melanogaster</i> Mondo (encoded by <i>Mio</i>) protein sequence with locations of introns, and phases indicated. Protein sequences were aligned with Clustal Omega. Locations of introns are indicated by ^ with the number referring to the phase of the codon interrupted by the intron. Introns at near identical locations, and of the same phase are boxed, with solid boxes indicated very similar locations, while dotted boxes are similar.</p

Consensus sequences for MCR1-6, bHLH-Zip and DCD domains in mammalian MondoA and ChREBP protein sequences.

<p>Consensus sequences from 10 mammalian ChREBP and MondoA protein sequences of Mondo Conserved Regions (MCR1-6), basic helix-loop helix leucine-zipper (bHLH-Zip) and the dimerization and cytoplasmic localization (DCD) domains are displayed by WebLogos. Numbers below residues indicate position in alignments of the 10 mammalian ChREBP or MondoA sequences. Heights of letters indicate abundance of that residue in the 10 sequences. Color of residues indicate chemical properties, with green being polar amino acids (G, S, T, Y, C, Q, and N), blue are basic (K, R, and H), red are acidic (D and E) and black are hydrophobic (A, V, L, I, P, W, F, and M).</p

Comparison of the average JS Divergence scores for domains in MondoA and ChREBP protein sequences.

<p>Comparison of the average JS Divergence scores for domains in MondoA and ChREBP protein sequences.</p

Variability in MondoA and ChREBP protein sequences.

<p>JS Divergence scores across the alignment of MondoA and ChREBP protein sequences. Plots of JS Scores for MondoA, ChREBP and combined MondoA and ChREBP protein sequences are shown. JS Scores for each position are presented in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0149682#pone.0149682.s017" target="_blank">S5 Table</a>. A schematic organization of the domains in MondoA and ChREBP is shown below the plot. Alignment of sequences and locations of domains are shown in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0149682#pone.0149682.s007" target="_blank">S7 Fig</a>.</p