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An α subunit-deficient form of eukaryotic protein synthesis initiation factor eIF-2 from rabbit reticulocyte lysate and its activity in ternary complex formation

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Abstract

Eukaryotic protein synthesis initiation factor eIF-2 is usually isolated as a heterotrimer (αβγ). By use of Sephacryl S-300 fractionation an α subunit-deficient form of eIF-2 was identified in impure preparations from rabbit reticulocyte lysate and it appeared in these preparations to be still active in formation of the ternary complex (eIF-2.GTP.Met-tRNAi). Subsequently α subunit-deficient eIF-2 was further purified and this appeared to have retained ternary complex forming activity. Together with a suggested lack of involvement of the β subunit this implies that the α subunit was not required for activity and the γ subunit bound both GTP and Met-tRNAi in formation of the ternary complex. The identification and study of α subunit-deficient eIF-2 thus elucidated the involvement of the subunits in binding of GTP and Met-tRNAi to produce the ternary complex in polypeptide chain initiation.

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  1. Department of Biochemistry, University of the Witwatersrand, Johannesburg, South Africa

    Michael Frank Mouat & Keith Manchester

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  1. Michael Frank Mouat
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  2. Keith Manchester
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Mouat, M.F., Manchester, K. An α subunit-deficient form of eukaryotic protein synthesis initiation factor eIF-2 from rabbit reticulocyte lysate and its activity in ternary complex formation. Mol Cell Biochem 183, 69–78 (1998). https://doi.org/10.1023/A:1006829615464

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