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Zinc7beret

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R, K3L or vIF2a, demonstrating that K3 and vIF2a had no effect on yeast cell growth (Figure 2A). In contrast, induction of PKR expression was toxic in the vector-transformed yeast, whereas the toxicity was suppressed by co-expression of K3L or vIF2a (Figure 2B). Based on the homology of vIF2a with eIF2a throughout the entire ORF we tested whether suppression of PKR toxicity might be caused by the
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R, K3L or vIF2a, demonstrating that K3 and vIF2a had no effect on yeast cell growth (Figure 2A). In contrast, induction of PKR expression was toxic in the vector-transformed yeast, whereas the toxicity was suppressed by co-expression of K3L or vIF2a (Figure 2B). Based on the homology of vIF2a with eIF2a throughout the entire ORF we tested whether suppression of PKR toxicity might be caused by the
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Ultiple eukaryotes was noted. During the second iteration, this region of similarity to eIF2a was extended to amino acid position 253 of vIF2a. Secondly, multiple sequence alignments including vIF2a from many ranaviruses and eIF2a from a diverse set of eukaryotes showed conservation of amino acids outside the S1 domain: 8 amino acids are 100 conserved among the sequences (Figure 1, red background
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With 4 substitution rate categories. The proportion of invariable sites and the gamma shape parameter were estimated from the data. We used 10 random starting trees, and subtree pruning and regrafting (SPR) [89] to search tree space. Both tree topology and branch lengths were optimized to maximize the likelihood. Branch support was estimated using 100 bootstrap replicates, and by calculating an ap
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D found in some eIF2a sequences: light blue. Secondary structure elements as reported for human eIF2a [41] are shown below the sequences: b-strand: red arrow; ahelix: blue box. Vertical arrows indicate boundaries between S1, helical, and C-terminal domains in eIF2a. Secondary structure elements that were predicted for RCV-Z and ATV vIF2a using Porter are shown above the alignments [55]. Cysteines