title: Chiral-selective aminoacylation of an RNA minihelix.
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.
authors.affiliation: Skaggs Institute for Chemical Biology, Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
authors.forename: Koji
authors.initials: K
authors.lastname: Tamura
authors.forename: Paul
authors.initials: P
authors.lastname: Schimmel
mesh_terms: D000215:Acylation; D000409:Alanine / Q000378:metabolism; D000596:Amino Acids / Q000737:chemistry / Q000378:metabolism*; D003855:Deoxyribose / Q000032:analysis; D007930:Leucine / Q000378:metabolism; D009690:Nucleic Acid Conformation; D009838:Oligodeoxyribonucleotides / Q000737:chemistry / Q000378:metabolism; D009841:Oligonucleotides / Q000737:chemistry / Q000378:metabolism*; D009843:Oligoribonucleotides / Q000737:chemistry / Q000378:metabolism; D010649:Phenylalanine / Q000378:metabolism; D012343:RNA, Transfer / Q000737:chemistry / Q000378:metabolism*; D012346:RNA, Transfer, Amino Acyl / Q000737:chemistry / Q000378:metabolism*; D012266:Ribose / Q000032:analysis; D013237:Stereoisomerism
chemical_list: D000596:Amino Acids; D009838:Oligodeoxyribonucleotides; D009841:Oligonucleotides; D009843:Oligoribonucleotides; D012346:RNA, Transfer, Amino Acyl; D010649:Phenylalanine; D003855:Deoxyribose; D012266:Ribose; D012343:RNA, Transfer; D007930:Leucine; D000409:Alanine