ArticlemicroPublication biology2025
Identification of Aspartyl-tRNA Synthetase as Co-purifying with Wheat Germ eIF2.
Article in microPublication biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Eukaryotic translation initiation factor 2 (eIF2) is among the best-studied of the translation initiation factors, but early preparations from wheat germ consistently showed a co-purifying protein of ~61kDa. As this protein was never identified, we revisited the question of its identity using mass spectrometry on an archived Coomassie-stained and dried gel of eIF2 purified in 1991. The co-purifying protein, aspartyl-tRNA synthetase, is notable for serving as a receptor for the R enantiomer of β-aminobutyric acid, with links to stress-induced eIF2α phosphorylation, highlighting the potential for stable "super complexes" connecting translation initiation with stress responses.
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