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Protein synthesis in rabbit reticulocytes XXII+: a heat stable dialyzable factor (EIF-I*) modulates Met-tRNAf binding to EIF-1



Protein synthesis in rabbit reticulocytes XXII+: a heat stable dialyzable factor (EIF-I*) modulates Met-tRNAf binding to EIF-1



Biochemical and Biophysical Research Communications 82(3): 1019-1027



The peptide chain initiation factor EIF-1 forms a ternary complex, Met-tRNAf.cntdot.EIF-1.cntdot.GTP in the absence of Mg2+ and the preformed complex is stable to Mg2+. With homogeneous preparations of EIF-1, addition of Mg2+ during the initial formation of the ternary complex strongly inhibits the complex formation. A heat stable dialyzable factor (EIF-1*) which mostly remains associated with the high MW protein complex, EIF-2 (TDF) during purification of the peptide chain initiation factors, was purified using a phenol extraction procedure. EIF-1* restores the Met-tRNAf binding activity of EIF-1* in the presence of 1 mM Mg2+; in the presence of EIF-1*, Met-tRNAf binding by EIF-1 shows a sharp Mg2+ optimum around 1 mM. EIF-1* is heat stable, alkali stable, dialyzable and pronase sensitive. The same EIF-1* preparation also strongly inhibits Met-tRNAf binding to EIF-1 in the absence of Mg2+ and stimulates protein synthesis in a mRNA-dependent rabbit reticulocyte lysate system.

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Accession: 068525138

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PMID: 250438

DOI: 10.1016/0006-291x(78)90885-9


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