Chain Initation Factor 3 Crosslinks to E. coli 30S and 50S Ribosomal Subunits and Alters the UV Absorbance Spectrum of 70S Ribosomes

The authors report a direct procedure to determine the proteins near the IF-3 binding site in purified 30S and 50S ribosomal subunits. The cleavable crosslinking reagent, 2-iminothiolane, was used to crosslink IF-3 in place to both 30S and 50S subunits. Ribosomal proteins S9/S11, S12, L2, L5 and L17...

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Bibliographic Details
Published in:Nucleic acids research 1982-01, Vol.10 (18), p.5681-5693
Main Authors: Chaires, J B, Hawley, DA, Wahba, A J
Format: Article
Language:English
Subjects:
Escherichia coli
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Summary:The authors report a direct procedure to determine the proteins near the IF-3 binding site in purified 30S and 50S ribosomal subunits. The cleavable crosslinking reagent, 2-iminothiolane, was used to crosslink IF-3 in place to both 30S and 50S subunits. Ribosomal proteins S9/S11, S12, L2, L5 and L17 were found, by this approach, to be in close proximity to the factor in purified IF-3-subunit complexes. In addition, IF-3 was shown to alter the ultraviolet absorbance spectrum of E. coli 70S ribosomes at 10 mM Mg super(2+). The results are taken to indicate a conformational change in the 70S ribosome induced by IF-3.
ISSN:0305-1048