An Improved Technique for the Analysis of Ribonucleoprotein Fragments from Escherichia coli 30S Ribosomes

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Abstract
30S ribosomal subunits from Escherichia coli were hydrolyzed with ribonuclease T1, and the ribonucleoprotein fragments produced were fractionated on a 5% polyacrylamide/0.5% agarose composite gel. Two main breakdown products were observed corresponding in size to about 20% and 60% of the intact 30S particle. Each fraction from the 5% composite gel was subjected to protein analysis on a periodatesoluble 15% polyacrylamide gel, run in the detergent Sarkosyl. The smaller ribonucleotprotein fragment was found to contain only four of the 30S ribosomal proteins, and these were present in equimolar amounts. The larger fragment had a complex protein composition; it was deficient in the four proteins contained in the smaller fragment, and was considerably enriched in the largest 30S protein. The results show a striking correlation with Nomura's “assembly map” of the 30S particle.

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