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Science 27 August 2004:
Vol. 305. no. 5688, p. 1253
DOI: 10.1126/science.1099141
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Chiral-Selective Aminoacylation of an RNA Minihelix

Koji Tamura and Paul Schimmel*

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.

The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.

* To whom correspondence should be addressed. E-mail: schimmel{at}scripps.edu

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