PMID: 7526895Jun 1, 1994Paper

The non-enzymatic specific amino-acylation of transfer RNA at high pressure

International Journal of Biological Macromolecules
A KrzyzaniakJ Jurczak

Abstract

This paper shows that the phenylalanine-specific tRNA of Escherichia coli as well as the yellow lupin methionine initiator tRNAMet can be charged specifically with phenylalanine and methionine, respectively, in the absence of specific aminoacyl-tRNA synthetases, under high pressure of a maximum of 6 kbar (1 bar = 10(5) Pa; 1 atm = 1.01 x 10(5) Pa). The esterification reaction takes places at the 3' end of the tRNA molecules. The yield of Phe-tRNAPhe or Met-tRNAMet at high pressure is approximately 10 times lower than that of the enzymatic aminoacylation reaction. This reaction seems to be specific, and mis-aminoacylation of tRNAPhe and tRNAMet with serine is negligible. It is well known that tRNA undergoes conformational changes during interaction with an aminoacyl-tRNA synthetase. Similarly, on the basis of circular dichroism spectra, we showed that the conformation of tRNA at high pressure differs slightly from its original A-RNA form. Therefore, it can be speculated that the chargeable conformation of tRNA induced by the aminoacyl-tRNA synthetase during enzymatic aminoacylation and the one created at high pressure are similar and are most probably formed by a dehydration mechanism. We think that the 'unique' tertiary structu...Continue Reading

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Citations

Jan 27, 2015·Current Opinion in Biotechnology·Markus A KellerMarkus Ralser
Jun 9, 2006·The FEBS Journal·Malgorzata Giel-Pietraszuk, Jan Barciszewski
Sep 14, 2018·Science Translational Medicine·Yun-Ruei KaoBritta Will
Mar 20, 2010·Biochemical Society Transactions·Matthew J BelousoffAda Yonath
Dec 6, 2019·Chemical Reviews·Marie-Christine MaurelGuy Hervé

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