PMID:7493319

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Citation

Yap, LP and Musier-Forsyth, K (1995) Transfer RNA aminoacylation: identification of a critical ribose 2'-hydroxyl-base interaction. RNA 1:418-24

Abstract

To understand the relationship between tRNA architecture and specific aminoacylation by aminoacyl-tRNA synthetases, we performed kinetic assays of Escherichia coli tRNA(Pro) molecules containing single deoxynucleotide substitutions. We identified an important 2'-hydroxyl group at position U8 (of 22 positions probed). Chemical modification studies showed that this 2'-hydroxyl interacts with either the N1 or the exocyclic amine of G46 in a hydrogen bonding interaction that contributes 1.8 kcal/mol to the free energy of activation for aminoacylation. Molecular modeling of tRNA(Pro) supports the existence of this interaction. This is the first study to identify a specific ribose 2'-hydroxyl-base interaction in the core region of a tRNA molecule that makes a thermodynamically significant contribution to aminoacylation.

Links

PubMed PMC1482412

Keywords

Acylation; Amino Acyl-tRNA Synthetases/metabolism; Base Sequence; Deoxyribonucleotides; Escherichia coli/genetics; Models, Molecular; Molecular Sequence Data; Nucleic Acid Conformation; RNA, Transfer, Pro/chemistry; RNA, Transfer, Pro/genetics; RNA, Transfer, Pro/metabolism; Ribose; Substrate Specificity; Thermodynamics; Uridine

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