Aug 31, 2004

Chiral-selective aminoacylation of an RNA minihelix

Science
Koji Tamura, P Schimmel

Abstract

Amino acids in natural proteins have a chiral, asymmetric center at the alpha carbon that is of the L-configuration. The sugar backbone of natural RNAs are also homochiral, but of the D-configuration. Because protein synthesis requires the aminoacylation of RNA, it is this step that could have provided chiral selectivity. Here we show that an RNA minihelix was aminoacylated by an aminoacyl-phosphate-D-oligonucleotide with a clear preference for L- as opposed to D-amino acids. A mirror-image RNA system showed the opposite selectivity. These results suggest the possibility that the selection of L-amino acids for proteins was determined by the stereochemistry of RNA.

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Mentioned in this Paper

Molecular Stereochemistry
RNA Conformation
Amino Acids, I.V. solution additive
Phosphate Measurement
Transfer RNA
Acylation
Abufne
Protein Biosynthesis
Ribose
Oligonucleotides

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