Effect of uridine dethiolation in the anticodon triplet of tRNA(Glu) on its association with tRNA(Phe).

Journal of Biomolecular Structure & Dynamics
C HoussierH Grosjean

Abstract

The effect of U(34) dethiolation on the anticodon-anticodon association between E. coli tRNA(Glu) and yeast tRNA(Phe) has been studied by the temperature jump relaxation technique. An important destabilization upon replacement of the thioketo group of s2U(34) by a keto group, was revealed by a lowering of melting temperature of about 20 degrees C. The measured kinetic parameters indicated that this destabilization effect was originated in an increase of dissociation and a decrease of association rate constants by a factor of 4 to 5. Modifications in both stacking interactions and flexibility in the anticodon loop would be responsible for this effect.

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Citations

Aug 13, 2011·Cellular and Molecular Life Sciences : CMLS·Barbara NawrotMarkus Düchler
Nov 20, 2002·Journal of Biomolecular Structure & Dynamics·Uddhavesh B SonavaneRavindra Tewari
Jan 11, 1994·Nucleic Acids Research·K WatanabeK Miura
Jan 13, 2004·Nucleic Acids Research·Paul F Agris
Mar 5, 2009·Microbiology and Molecular Biology Reviews : MMBR·John F Atkins, Glenn R Björk
Mar 10, 2017·RNA Biology·Raffael Schaffrath, Sebastian A Leidel
Jan 8, 1999·Journal of Molecular Biology·P C Durant, D R Davis
Dec 10, 1998·Nature Structural Biology·E V Puglisi, J D Puglisi
Dec 18, 2002·The Journal of Biological Chemistry·Michaël RyckelynckMagali Frugier
Dec 12, 2018·Biochimica Et Biophysica Acta. Gene Regulatory Mechanisms·Jillian Ramos, Dragony Fu

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