Abstract
The complex of 5S RNA and proteins L18 and L25 from Escherichia coli has proved useful for studying both the chemistry of protein-RNA interactions and for examining cooperative assembly effects within ribosomes (reviewed by Garrett et al. 1981, 1984). It has the following advantages over most other protein-RNA complexes for such seminal studies: Both RNA and proteins are available in large quantities; the RNA is relatively small and homogeneous; the RNA secondary structure has been determined both experimentally and by comparing sequences to detect coordinated base changes; and the proteins are small and of known sequence. The current disadvantage is that insufficient protein sequences are available for localizing conserved amino acids or peptide sequences.
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Christiansen, J., Garrett, R.A. (1986). How Do Protein L18 and 5S RNA Interact?. In: Hardesty, B., Kramer, G. (eds) Structure, Function, and Genetics of Ribosomes. Springer Series in Molecular Biology. Springer, New York, NY. https://doi.org/10.1007/978-1-4612-4884-2_15
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DOI: https://doi.org/10.1007/978-1-4612-4884-2_15
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