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. 2010 Feb 9;5(2):e9114. doi: 10.1371/journal.pone.0009114

Figure 1. eIF4G isoforms from Saccharomyces cerevisiae.

Figure 1

(A) Schematic of the two eIF4G isoforms from S. cerevisiae (encoded by TIF4631 and TIF4632). Experimentally verified domains of interaction are shown as colored blocks with binding partners indicated on the right and boundaries (amino acid positions) below [12], [19], [87], [88], [89], [90]. RNA (RS)  =  Arginine-Serine rich RNA binding domain; 4E HPO  =  Y(X)4LΦ motif of eIF4E (Φ  =  hydrophobic amino acid). (B) A pairwise alignment of TIF4631 and TIF4632 protein sequences was generated using MUSCLE [78] and a schematic of the consensus is shown. Domain homologies are indicated as a percentage of amino acid identity (similarity). Alignment quality (based on BLOSUM62 Scores; key on right) is indicated in the heat map below, where yellow is high quality, blue is low quality, and white is a gap (where sequence in the consensus originates from a single isoform). The score at each residue represents a sliding window average of 3 amino acids (See Materials and Methods).