PMID: 7027253Jul 1, 1981Paper

Removal of beta subunit of the eukaryotic polypeptide chain initiation factor 2 by limited proteolysis

Proceedings of the National Academy of Sciences of the United States of America
K I MitsuiS Ochoa

Abstract

It is generally considered that the eukaryotic polypeptide chain initiation factor 2 (eIF-2) from rabbit reticulocytes consists of three nonidentical subunits termed alpha, beta, and gamma, in order of increasing molecular weight. However, a recent report [Stringer, E. A., Chaudhuri, A., Valenzuela, D. & Maitra, U. (1980) Proc. Natl. Acad. Sci. USA 77, 3356-3359] suggested that this factor is made up of only two subunits. In this paper we show that limited proteolysis of rabbit reticulocyte eIF-2 leads to loss of the beta subunit. This modified eIF-2 has the same activity as the native factor in promoting ternary (eIF-2.GTP.Met-tRNAi) and 40S (eIF-2.GTP.Met-tRNAi.40S ribosome) initiation complex formation. Like native eIF-2, the protease-treated factor can restore translation in heme-deficient lysates. On the other hand, the treated factor is less stable than the native protein.

References

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Oct 1, 1979·Proceedings of the National Academy of Sciences of the United States of America·A DasN K Gupta
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Citations

Jan 1, 1991·Pharmacology & Therapeutics·S J Morley, G Thomas
Mar 1, 1983·Proceedings of the National Academy of Sciences of the United States of America·J SiekierkaS Ochoa
May 1, 1988·Proceedings of the National Academy of Sciences of the United States of America·B DattaN K Gupta
May 17, 2011·Biochemistry. Biokhimii︠a︡·E A Stolboushkina, M B Garber
Nov 10, 2009·FEBS Letters·Emmanuelle SchmittYves Mechulam
Jun 1, 1983·Archives of Biochemistry and Biophysics·S Ochoa
Aug 15, 1990·Archives of Biochemistry and Biophysics·D D AnthonyW C Merrick
Apr 5, 2016·Nature Communications·Valentina GandinIvan Topisirovic
Feb 6, 2004·The Journal of Biological Chemistry·Laure YatimeYves Mechulam
Jun 1, 1992·Microbiological Reviews·W C Merrick

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