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Science 24 June 1988:
Vol. 240. no. 4860, pp. 1751 - 1758
DOI: 10.1126/science.3381099
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Articles

Science, Vol 240, Issue 4860, 1751-1758
Copyright © 1988 by American Association for the Advancement of Science

articles

A specific amino acid binding site composed of RNA

M Yarus

Department of Molecular, Cellular, and Developmental Biology, University of Colorado, Boulder 80309.

A specific, reversible binding site for a free amino acid is detectable on the intron of the Tetrahymena self-splicing ribosomal precursor RNA. The site selects arginine among the natural amino acids, and prefers the L- to the D-amino acid. The dissociation constant is in the millimolar range, and amino acid binding is at or in the catalytic rG splicing substrate site. Occupation of the G site by L-arginine therefore inhibits splicing by inhibiting the binding of rG, without inhibition of later reactions in the splicing reaction sequence. Arginine binding specificity seems to be directed at the side chain and the guanidino radical, and the alpha-amino and carboxyl groups are dispensable for binding. The arginine site can be placed within the G site by structural homology, with consequent implications for RNA-amino acid interaction, for the origin of the genetic code, for control of RNA activities, and for further catalytic capabilities for RNA.


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