| Interacting proteins: P62495 and P05198 |
Pubmed |
SVM Score :0.0 |
| We found that the vast majority of translation initiation factors ( eIF 2 , eIF2B , eIF 3 , eIF4A1 , eIF 5 and eIF5B ) , all three elongation factors ( eEF1A , eEF1B and eEF 2 ) and the termination factor eRF 1 are strictly excluded from nuclei . ^^^ |
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| Interacting proteins: P62495 and P05198 |
Pubmed |
SVM Score :0.0 |
| Eukaryotic initiation factor eIF 2 and eukaryotic recycling factor eRF from neuroblastoma cells . eIF 2 purified from neuroblastoma cells consists of three subunits , which appear to be of molecular weight identical to those of the subunits of rabbit reticulocyte eIF 2 . ^^^ A protein fraction has been isolated from neuroblastoma cells with characteristics similar to eRF from reticulocytes : stimulation of amino acid incorporation in a hemin deprived reticulocyte lysate , the removal of GDP from eIF 2 GDP complexes , a 4 5 fold stimulatory effect in a two step reaction measuring 40 S preinitiation complex formation and a 3 3 . 5 fold stimulation in the methionyl puromycin synthesis . ^^^ |
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| Interacting proteins: P62495 and P05198 |
Pubmed |
SVM Score :0.0 |
| Mode of action of eRF , an eIF 2 recycling factor from rabbit reticulocytes involved in GDP / GTP exchange . ^^^ In the latter assay a catalytic use of eIF 2 occurs provided that eRF is present . eRF forms a complex with eIF 2 which results in a decrease of the affinity of eIF 2 for GDP , giving it the properties of a GDP / GTP exchange factor . ^^^ The model stresses the catalytic use of eIF 2 in initiation provided that conditions are met for GDP / GTP exchange by a transient complex formation between eIF 2 and eRF . ^^^ On the other hand , it is shown that phosphorylation of eIF 2 by the hemin regulated inhibitor ( HRI ) abolishes the recycling of eIF 2 , by the formation of another stable complex comprising eIF 2 alpha P , GDP and eRF . . ^^^ |
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