An article Domain II of the translation elongation factor eEF1A is required for Gcn2 kinase inhibition WOS:000534662900001 published article about TRANSFER-RNA-BINDING; UNCHARGED TRANSFER-RNA; PROTEIN-KINASE; FACTOR 1A; SACCHAROMYCES-CEREVISIAE; STRUCTURAL BASIS; FULL ACTIVATION; INITIATION; ACID; RIBOSOME in [Ramesh, Rashmi; Sattlegger, Evelyn] Massey Univ, Sch Nat & Computat Sci, Albany Highway,Gate 4,Bldg 11, Auckland 0632, New Zealand; Linkoping Univ, Dept Biomed & Clin Sci BKV, Inst Clin & Expt Biol, Cellbiol Floor 12, S-58185 Linkoping, Sweden in 2020.0, Cited 59.0. Category: Triazoles. The Name is 1H-1,2,4-Triazol-5-amine. Through research, I have a further understanding and discovery of 61-82-5
The signalling pathway governing general control nonderepressible (Gcn)2 kinase allows cells to cope with amino acid shortage. Under starvation, Gcn2 phosphorylates the translation initiation factor eukaryotic translation initiation factor (eIF)2 alpha, triggering downstream events that ultimately allow cells to cope with starvation. Under nutrient-replete conditions, the translation elongation factor eEF1A binds Gcn2 to contribute to keeping Gcn2 inactive. Here, we aimed to map the regions in eEF1A involved in binding and/or regulating Gcn2. We find that eEF1A amino acids 1-221 and 222-315, containing most of domains I and II, respectively, bind Gcn2 in vitro. Overexpression of eEF1A lacking or containing domain III impairs eIF2 alpha phosphorylation. While the latter reduces growth under starvation similarly to eEF1A lacking domain I, the former enhances growth in a Gcn2-dependent manner. Our studies suggest that domain II is required for Gcn2 inhibition and that eEF1A lacking domain III mainly affects the Gcn2 response pathway downstream of Gcn2.
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Reference:
Article; Safari, Niloufar; Shirini, Farhad; Tajik, Hassan; Journal of Molecular Structure; vol. 1201; (2020);,
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