Title : Role of reversing factor in the inhibition of protein synthesis initiation by oxidized glutathione.

Pub. Date : 1988 Oct 25

PMID : 3170604






4 Functional Relationships(s)
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1 The inhibitions of protein synthesis initiation in heme-deficient reticulocyte lysates and in GSSG-treated hemin-supplemented lysates are both characterized by the activation of heme-regulated eIF-2 alpha kinase, which phosphorylates the alpha-subunit of eukaryotic initiation factor (eIF-2). Glutathione Disulfide eukaryotic translation initiation factor 2 subunit beta Homo sapiens
2 The inhibitions of protein synthesis initiation in heme-deficient reticulocyte lysates and in GSSG-treated hemin-supplemented lysates are both characterized by the activation of heme-regulated eIF-2 alpha kinase, which phosphorylates the alpha-subunit of eukaryotic initiation factor (eIF-2). Glutathione Disulfide eukaryotic translation initiation factor 2 subunit beta Homo sapiens
3 RF inactivation in GSSG-induced inhibition appears to be due to two separate but additive effects: (i) the formation of the phosphorylated 15 S RF complex, RF.eIF-2(alpha P), and (ii) the formation of disulfide complexes which inhibit RF activity. Glutathione Disulfide eukaryotic translation initiation factor 2 subunit beta Homo sapiens
4 RF inactivation in GSSG-induced inhibition appears to be due to two separate but additive effects: (i) the formation of the phosphorylated 15 S RF complex, RF.eIF-2(alpha P), and (ii) the formation of disulfide complexes which inhibit RF activity. Glutathione Disulfide eukaryotic translation initiation factor 2 subunit beta Homo sapiens