PMID:11697733

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Citation

Schlosser, A, Nawrot, B, Grillenbeck, N and Sprinzl, M (2001) Fluorescence-monitored conformational change on the 3'-end of tRNA upon aminoacylation. J. Biomol. Struct. Dyn. 19:285-91

Abstract

Fluorescent tRNAs species with formycine in the 3'-terminal position (tRNA-CCF) were derived from Escherichia coli tRNA(Val). Thermus thermophilus tRNA(Aap) and Thermus thermophilus tRNA(Phe). The fluorescence of formycine was used to monitor the conformational changes at the 3'-terminus of tRNA caused by aminoacylation and hydrolysis of aminoacyl residue from aminoacyl-tRNAs. An increase of about 15% in the fluorescence intensity was observed after aminoacylation of the three tRNA-CCF. This change in fluorescence amplitude that is reversed by hydrolysis of the aminoacyl residue, does not depend on the structure of the amino acid or tRNA sequence. A local conformational change at the 3'-terminal formycine probably involving a partial destacking of the base moiety in the ACCF end takes place as a consequence of aminoacylation. A structural change at the 3'-terminus of tRNA induced by attachment and detachment of the acyl residue may be important in controlling the substrate/product relationship in reactions in which tRNA participates during protein biosynthesis.

Links

PubMed Online version:10.1080/07391102.2001.10506739

Keywords

Chromatography, High Pressure Liquid; Escherichia coli/chemistry; Fluorescent Dyes/chemistry; Formycins/chemistry; Magnetic Resonance Spectroscopy; Nucleic Acid Conformation; RNA, Transfer, Amino Acyl/chemistry; RNA, Transfer, Asp/chemistry; RNA, Transfer, Phe/chemistry; RNA, Transfer, Val/chemistry; Ribonucleotides/chemistry; Thermus thermophilus/chemistry

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