Nucleic Acids Research, 1978, Vol. 5, No. 6 1753-1766
© 1978
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Fragment of protein L18 from the Escherichia coli ribosome that contains the 5S RNA binding site
Max-Planck-Institut für Molekulare Genetik, Abt. Wittmann Berling-33, GFR and Department of Genetics, University of Birmingham UK
$To whom correspondence should be addressed
Received April 12, 1978.
A fragment of ribosomal protein L18 was prepared by limited trypsin digestion of a specific complex of L18 and 5S RNA. It was characterised for sequence and the very basic N-terminal region of the protein was found to be absent. No smaller resistant fragments were produced. 5S RNA binding experiments indicated that the basic N-terminal region, from amino acid residues 1 to 17, was not important for the L18-5S RNA association.
Under milder trypsin digestion conditions three resistant fragments were produced from the free protein. The largest corresponded to that isolated from the complex. The smaller ones were trimmed slightly further at both N- and C-terminal ends. These smaller fragments did not reassociate with 5S RNA.
It was concluded on the basis of the trypsin protection observations and the 5S RNA binding results that the region extending from residues 18 to 117 approximates to the minimun amount of protein required for a specific and stable protein-RNA interaction.
The accessibility of the very basic N-terminal region of L18, in the L18-5S RNA complex, suggests that it may be involved, in some way, in the interaction of 5S RNA with 23S RNA.
*Present address: Thimann Laboratories, University of California, Santa Cruz.
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