SUI2 cDNA ORF clone, Saccharomyces cerevisiae S288C

Life with 6000 genes.
Goffeau A, Barrell BG, Bussey H, Davis RW, Dujon B, Feldmann H, Galibert F, Hoheisel JD, Jacq C, Johnston M, Louis EJ, Mewes HW, Murakami Y, Philippsen P, Tettelin H, Oliver SG
Science (New York, N.Y.)274(5287)546, 563-7(1996 Oct)

Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.
Galibert F, Alexandraki D, Baur A, Boles E, Chalwatzis N, Chuat JC, Coster F, Cziepluch C, De Haan M, Domdey H, Durand P, Entian KD, Gatius M, Goffeau A, Grivell LA, Hennemann A, Herbert CJ, Heumann K, Hilger F, Hollenberg CP, Huang ME, Jacq C, Jauniaux JC, Katsoulou C, Karpfinger-Hartl L
The EMBO journal15(9)2031-49(1996 May)

These data uncover competition between eIF2B and eIF5 for eIF2-GTP/Met-tRNAi ternary complexes and identify that phosphorylated eIF2-GTP translation initiation intermediate complexes can be inhibited by eIF2B.
Title: Fail-safe control of translation initiation by dissociation of eIF2? phosphorylated ternary complexes.

Translation elongation factor 1A mutants with altered actin bundling activity show reduced aminoacyl-tRNA binding and alter initiation via eIF2alpha phosphorylation.
Title: Translation elongation factor 1A mutants with altered actin bundling activity show reduced aminoacyl-tRNA binding and alter initiation via eIF2? phosphorylation.

Data indicate that Cdc123 is a specific assembly factor for eukaryotic translation initiation factor 2 (eIF) subunit alpha (sui2), subunit beta (sui3) and subunit gamma (GCD11), which is indispensable for the onset of protein synthesis.
Title: Translation initiation requires cell division cycle 123 (Cdc123) to facilitate biogenesis of the eukaryotic initiation factor 2 (eIF2).

study found that phosphorylation of eIF2alpha by methylglyoxal occurred independently of the target of rapamycin (TOR) pathway
Title: Methylglyoxal activates Gcn2 to phosphorylate eIF2alpha independently of the TOR pathway in Saccharomyces cerevisiae.

Mutationally disrupting the hydrophobic network in various ways constitutively activates eIF2alpha phosphorylation in vivo and bypasses the requirement for a key tRNA binding motif (m2) and Thr-882 in Gcn2.
Title: A network of hydrophobic residues impeding helix alphaC rotation maintains latency of kinase Gcn2, which phosphorylates the alpha subunit of translation initiation factor 2.