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Nucleic Acids Research, 1977, Vol. 4, No. 2 491-499
© 1977

Articles

Isolation of ribosomal protein-RNA complexes by nitrocellulose membrane filtration: equilibrium binding studies

Eleanor Spicer+, Jean Schwarzbauer and Gary R. Craven

Laboratory of Molecular Biology and Department of Genetics, University of Wisconsin Madison, Wl 53706, USA

Received January 20, 1977.

E. coli ribosomal proteins are retained by nitrocellulose filters. In contrast, 16S RNA passes through nitrocellulose filters. We have found that specific protein-RNA complexes involving single proteins also pass through nitrocellulose filters. Thus, by utilizing radioactively labeled r-proteins, nitrocellulose filtration can be used to study directly and sensitively the stoichiometry of r-protein-RNA association. The filtration process maintains near equilibrium conditions1, making it applicable to weak as well as strong protein-RNA associations. We have used nitrocellulose filtration to obtain saturation binding curves for the association of proteins S4, S7, S8 and S20 with 16S RNA. In each case, the stoichiometry of binding was one mole of protein or less per mole of RNA. The stoichiometry of protein S8 binding to 16S RNA measured by filtration is comparable to that observed by sucrose gradient centrifugation. Association constants for the binding of proteins S4, S8 and S20 to 16S RNA have been determined by analysis of the saturation binding curves and were found to range from .3–6 x 107 M–1

+Present Address: Department of Molecular Biophysics, and Biochemistry, Yale University, 333 Cedar Street, New Haven, Connecticut 06510


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