The Interconversion of Conformers of Phenylalanyl-tRNA with Different Affinity to 70S Ribosomes of Escherichia Coli

Overview

Journal Nucleic Acids Res

Publisher Oxford University Press

Specialty Biochemistry

Date 1978 May 1

PMID 351562

Citations 2

Authors

S V Kirillov

V B Odinzov

Affiliations

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Abstract

Earlier the existence of two conformers of Phe-tRNAPhe of E. coli was demonstrated because one of them yields complexes with 70S-poly(U) of extremely high affinity and the other with at least a 105 lower binding constant. We denote the first conformer as HAC (high affinity conformer) and the second as LAC (low affinity conformer). This high difference in binding constants was used for studying the process of reversible interconversion of conformers of Phe-tRNAPhe. The transition kinetics of LAC to HAC in conditions when the latter is stable (in the presence of magnesium ions) was studied and a high value of activation energy (35 kcal/mole) found. The interconversion is the first order reaction and equilibrium does not depend of overall Phe-tRNA concentration.

Citing Articles

Carbodiimide modification analysis of aminoacylated yeast phenylalanine tRNA: evidence for change in the apex region.

Fritzinger D, Fournier M Nucleic Acids Res. 1982; 10(7):2419-37.

PMID: 7045810 PMC: 320620. DOI: 10.1093/nar/10.7.2419.

Study on conformational states of Escherichia coli tRNAPhe in solution by a modulation-free ESR-spectrometer.

Bondarev G, Isaev-Ivanov V, Kirillov S, Kleiner A, Lepekhin A, Odinzov V Nucleic Acids Res. 1982; 10(3):1113-26.

PMID: 6278435 PMC: 326226. DOI: 10.1093/nar/10.3.1113.

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