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Nucleic Acids Research, 1982, Vol. 10, No. 4 1327-1334
© 1982


MOLECULAR BIOLOGY

Specific interaction of one subunit of eukaryotic initiation factor eIF-3 with 18S ribosomal RNA within the binary complex, eIF-3.small ribosomal subunit, as shown by cross-linking experiments

Odd Nygård* and Peter Westermann{dagger}

Department of Cell Physiology, The Wenner-Gren Institute, University of Stockholm S-113 45 Stockholm, Sweden {dagger}Central Institute of Molecular Biology, Academy of Sciences of GDR 1115 Berlin-Buch, GDR

*To whom correspondence should be addressed

Received January 5, 1982. Accepted January 29, 1982.

Initiation factor eIF-3 from rat liver forms a binary complex with the small ribosomal subunit. Within this complex, 18S ribosomal RNA can be cross-linked to the 66 000 dalton subunit of eIF-3 by treating the complex with a short bifunctional reagent, diepoxybutane, with a distance of 4A between the reactive groups. In binary complexes containing eIF-3 premodified with the heterobifunctional reagent, methyl-p-azido-benzoylaminoacetimidate (10Å), the 66 000 dalton subunit of eIF-3 became covalently bound to 18S rRNA after irradiation of the complex with ultraviolet light. The involvement of only one of the eight eIF-3 subunits in the formation of the covalent RNA-protein complexes indicates a highly specific interaction between 18S rRNA and eIF-3 at the attachment site of the factor on the 40S subunit.


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