Browne CM, Samir P, Fites JS, Villarreal SA, Link AJ

Using affinity purifications coupled with mass spectrometry and yeast-2-hybrid assays, we show the Saccharomyces cerevisiae translation initiation factor complex eIF2B and the very-long-chain-fatty acid (VLCFA) synthesis keto-reductase enzyme YBR159W physically interact. The data shows the interaction is specifically between YBR159W and eIF2B and not between other members of the translation ...

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initiation or VLCFA pathways. A ybr159wΔ null strain has a slow growth phenotype and reduced translation rate but a normal GCN4 response to amino acid starvation. While YBR159W localizes to the ER membrane, subcellular fractionation experiments show that a fraction of eIF2B co-fractionates with lipid membranes in a YBR159W-independent manner. We show that a ybr159wΔ yeast strain and other strains with null mutations in the VLCFA pathway cause eIF2B to appear as numerous foci throughout the cytoplasm.

Date: Dec. 21, 2012

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