Binding of 50 S ribosomal subunit proteins to 23 S RNA of Escherichia coli
|Published in||Journal of Molecular Biology. 1974, vol. 88, no. 2, p. 553-7|
|Abstract||Each of the 50 S ribosomal subunit proteins of Escherichia coli was tested independently in two laboratories for its ability to bind specifically to 23 S RNA. Four new RNA-binding proteins, L1, L3, L4 and L13 were identified in this way. Consistent with earlier work, proteins L2, L6, L16, L20, L23 and L24 were found to interact directly and independently with 23 S RNA as well. No binding of L17 was detected, however, contrary to previous reports, and the results for L19 were variable. The molar ratio of protein and RNA in each complex was measured at saturation. Significant differences in binding stoichiometry were noted among the various proteins. In addition, saturation levels were found to be influenced by the state of both the RNA and the proteins.|
|Keywords||Bacterial Proteins — Centrifugation, Density Gradient — Electrophoresis — Escherichia coli — Molecular Weight — Protein Binding — RNA, Bacterial — RNA, Ribosomal — Sodium Dodecyl Sulfate|
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|GARRET, R A. et al. Binding of 50 S ribosomal subunit proteins to 23 S RNA of Escherichia coli. In: Journal of Molecular Biology, 1974, vol. 88, n° 2, p. 553-7. doi: 10.1016/0022-2836(74)90503-8 https://archive-ouverte.unige.ch/unige:10152|