Cross-linking of initiation factor IF3 to proteins of the Escherichia coli 30 S ribosomal subunit

Ronald L. Heimark, Lawrence Kahan, Kathleen Johnston, John W.B. Hershey, Robert R. Traut

Research output: Contribution to journalArticlepeer-review

43 Scopus citations

Abstract

Complexes of 30 S subunits and [14C]IF3 were allowed to react with the protein cross-linking reagents, N,N′-p-phenylenedimaleimide or dimethylsuberimidate. Non-cross-linked IF3 was removed from the complex by centrifugation in a buffer containing a high salt concentration, and the total protein was extracted from the pelleted particles. The mixture of cross-linked products was analyzed by radioimmunodiffusion with antisera prepared against all of the individual 30 S ribosomal proteins. Radioactivity was found in the precipitin bands formed with antisera against ribosomal proteins S1, S11, S12, S13, S19 and S21. The results show that IF3 was present in covalent cross-linked complexes containing those 30 S ribosomal proteins and imply that they comprise or are near the binding site for initiation factor IF3.

Original languageEnglish (US)
Pages (from-to)219-230
Number of pages12
JournalJournal of Molecular Biology
Volume105
Issue number2
DOIs
StatePublished - Aug 5 1976
Externally publishedYes

ASJC Scopus subject areas

  • Molecular Biology

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