Distinct epitopes in eukaryotic initiation factor 2 for binding of mRNA and for ternary complex formation with methionyl-tRNAf and GTP

Ronit Harary, Raymond Kaempfer*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

7 Scopus citations

Abstract

Eukaryotic initiation factor 2 (eIF-2) forms a ternary complex with methionyl-tRNAMetf and GTP on one hand, and it binds to a specific site in mRNA molecules on the other. Antibodies directed against eIF-2 were used to analyze these dual binding activities. A monoclonal antibody directed against the β-subunit of eIF-2, 5A4, is able to inhibit ternary complex formation as well as binding of mRNA, showing that this subunit is essential for both binding activities of eIF-2. However, a polyclonal antibody, PR1, is able to distinguish between these activities in the eIF-2 molecule. In the presence of PR1, binding of mRNA by eIF-2 is inhibited completely, yet ternary complex formation with methionyl-tRNAMetf and GTP is stimulated more than 5-fold. Apparently, specific antibodies to eIF-2 can induce a conformational change in inactive factor molecules that permits them to form ternary complexes. These results show that distinct epitopes in eIF-2 are involved in binding of mRNA and in ternary complex formation with methionyl-tRNAMetf and GTP.

Original languageEnglish
Pages (from-to)129-133
Number of pages5
JournalBiochimica et Biophysica Acta - Gene Structure and Expression
Volume1050
Issue number1-3
DOIs
StatePublished - 27 Aug 1990

Keywords

  • Antibodies against eIF-2
  • Eukaryotic initiation factor 2
  • Translational control
  • eIF-2 epitope
  • mRNA binding
  • methionyl-tRNA binding

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