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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Acylation
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Alanine / metabolism
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Amino Acids / chemistry
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Amino Acids / metabolism*
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Deoxyribose / analysis
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Leucine / metabolism
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Nucleic Acid Conformation
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Oligodeoxyribonucleotides / chemistry
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Oligodeoxyribonucleotides / metabolism
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Oligonucleotides / chemistry
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Oligonucleotides / metabolism*
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Oligoribonucleotides / chemistry
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Oligoribonucleotides / metabolism
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Phenylalanine / metabolism
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RNA, Transfer / chemistry
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RNA, Transfer / metabolism*
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RNA, Transfer, Amino Acyl / chemistry
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RNA, Transfer, Amino Acyl / metabolism*
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Ribose / analysis
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Stereoisomerism
Substances
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Amino Acids
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Oligodeoxyribonucleotides
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Oligonucleotides
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Oligoribonucleotides
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RNA, Transfer, Amino Acyl
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Phenylalanine
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Deoxyribose
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Ribose
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RNA, Transfer
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Leucine
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Alanine