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Nucleic Acids Research, 1977, Vol. 4, No. 10 3327-3340
© 1977

Articles

Ribosomal protein - nucleic acid interactions. I. Isolation of a polypeptide fragment from 30S protein S8 which binds to 16S rRNA

J. Bruce, E. J. Firpo and H. W. Schaup{dagger}

Department of Biochemistry and Biophysics, Oregon State University, Corvallis OR 97331, USA

{dagger}Author to whom correspondence should be addressed

Received July 19, 1977. Within the bacterial ribosome a large number of specific protein and rRNA interactions appear to be required for assembly of the particle and its subsequent function in protein synthesis. In this communication it is shown that it is possible to isolate cyanogen bromide digestion products from ribo-somal 30S protein S8 which will interact stoichiometrically with 16S rRNA. In addition to this a small binding polypeptide was generated from S8–16S rRNA complexes which were treated with proteinase K. The digestion of the complex yields a "protected" fragment of protein S8 which binds to 16S-rRNA. The isolated fragment will reassociate with 16S rRNA. It is not displaced by other 30S ribosomal proteins and blocks the binding of intact S8 to 16S rRNA. The size and possible structure of the S8 protein binding site are discussed and compared with the binding of cyanogen bromide digestion products which bind to 16S rRNA.


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