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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred

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1437-4315
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Volume 390, Issue 9

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Effect of a quaternary pentamine on RNA stabilization and enzymatic methylation

Armine Hayrapetyan
  • Institute of Pharmacy and Molecular Biotechnology, University of Heidelberg, Im Neuenheimer Feld 364, D-69120 Heidelberg, Germany
  • Other articles by this author:
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/ Henri Grosjean
  • Institute of Genetics and Microbiology, University Paris-Sud, CNRS UMR 8621, F-91405 Orsay, France
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/ Mark Helm
  • Institute of Pharmacy and Molecular Biotechnology, University of Heidelberg, Im Neuenheimer Feld 364, D-69120 Heidelberg, Germany
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Published Online: 2009-06-27 | DOI: https://doi.org/10.1515/BC.2009.096

Abstract

Extreme thermophiles produce unusually long polyamines, including the linear caldopentamine (Cdp) and the branched pentamine tetrakis(3-aminopropyl)-ammonium (Taa), with the latter containing a central quaternary ammonium moiety. Here we compare the interaction of these two pentamines with RNA by studying the heat denaturation, electrophoretic behavior, and ability of tRNA to be methylated in vitro by purified tRNA methyltransferases under various salt conditions. At concentrations in the micromolar range, branched Taa causes a considerable increase in the melting temperature (T m) of yeast tRNAPhe transcripts by >20°C, which is significantly greater than stabilization by the linear Cdp. In non-denaturing gel electrophoresis, strong and specific binding to Taa, but not to Cdp, was clearly observed for tRNAPhe. In both types of experiments, polyamines and monovalent metal ions competed for binding sites. Structural probing revealed no significant conformational changes in tRNA on Taa binding. In post-transcriptional in vitro methylation reactions, the formation of m2G/m2 2G by the methyltransferase Trm1p and of m1A by TrmIp were not affected or only slightly stimulated by polyamines. In contrast, Taa specifically inhibited Trm4p-dependent formation of m5C only in tRNAPhe, likely by occupying sites that are relevant to RNA recognition by the methyltransferase.

Keywords: biophysical; polyamines; thermal stabilization; tRNA; tRNA methyltransferase; UV melting

About the article

Corresponding author


Received: 2009-03-13

Accepted: 2009-04-29

Published Online: 2009-06-27

Published in Print: 2009-09-01


Citation Information: Biological Chemistry, Volume 390, Issue 9, Pages 851–861, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2009.096.

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