Effect of a quaternary pentamine on RNA stabilization and enzymatic methylation

Publikationstyp:
Zeitschriftenaufsatz
Metadaten:
Autoren
  • Armine Hayrapetyan
  • Henri Grosjean
  • Mark Helm
Autoren-URL
https://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=fis-test-1&SrcAuth=WosAPI&KeyUT=WOS:000269485600003&DestLinkType=FullRecord&DestApp=WOS_CPL
DOI
10.1515/BC.2009.096
eISSN
1437-4315
Externe Identifier
  • Clarivate Analytics Document Solution ID: 490FW
  • PubMed Identifier: 19558320
ISSN
1431-6730
Ausgabe der Veröffentlichung
9
Zeitschrift
BIOLOGICAL CHEMISTRY
Schlüsselwörter
  • biophysical
  • polyamines
  • thermal stabilization
  • tRNA
  • tRNA methyltransferase
  • UV melting
Paginierung
851 - 861
Datum der Veröffentlichung
2009
Status
Published
Titel
Effect of a quaternary pentamine on RNA stabilization and enzymatic methylation
Sub types
  • Article
Ausgabe der Zeitschrift
390

Datenquelle: Web of Science (Lite)

Andere Metadatenquellen:
Abstract
<jats:title>Abstract</jats:title> <jats:p>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 <jats:italic>in vitro</jats:italic> by purified tRNA methyltransferases under various salt conditions. At concentrations in the micromolar range, branched Taa causes a considerable increase in the melting temperature (<jats:italic>T</jats:italic> <jats:sub>m</jats:sub>) of yeast tRNA<jats:sup>Phe</jats:sup> transcripts by &gt;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 tRNA<jats:sup>Phe</jats:sup>. 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 <jats:italic>in vitro</jats:italic> methylation reactions, the formation of m<jats:sup>2</jats:sup>G/m<jats:sup>2</jats:sup> <jats:sub>2</jats:sub>G by the methyltransferase Trm1p and of m<jats:sup>1</jats:sup>A by TrmIp were not affected or only slightly stimulated by polyamines. In contrast, Taa specifically inhibited Trm4p-dependent formation of m<jats:sup>5</jats:sup>C only in tRNA<jats:sup>Phe</jats:sup>, likely by occupying sites that are relevant to RNA recognition by the methyltransferase.</jats:p>
Autoren
  • Armine Hayrapetyan
  • Henri Grosjean
  • Mark Helm
DOI
10.1515/bc.2009.096
eISSN
1437-4315
ISSN
1431-6730
Ausgabe der Veröffentlichung
9
Zeitschrift
bchm
Sprache
en
Online publication date
2009
Paginierung
851 - 861
Datum der Veröffentlichung
2009
Status
Published
Herausgeber
Walter de Gruyter GmbH
Herausgeber URL
http://dx.doi.org/10.1515/bc.2009.096
Datum der Datenerfassung
2022
Titel
Effect of a quaternary pentamine on RNA stabilization and enzymatic methylation
Ausgabe der Zeitschrift
390

Datenquelle: Crossref

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 tRNA(Phe) transcripts by >20 degrees 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 tRNA(Phe). 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 m(2)G/m(2)(2)G by the methyltransferase Trm1p and of m(1)A by TrmIp were not affected or only slightly stimulated by polyamines. In contrast, Taa specifically inhibited Trm4p-dependent formation of m(5)C only in tRNA(Phe), likely by occupying sites that are relevant to RNA recognition by the methyltransferase.
Addresses
  • Institute of Pharmacy and Molecular Biotechnology, University of Heidelberg, Heidelberg, Germany.
Autoren
  • Armine Hayrapetyan
  • Henri Grosjean
  • Mark Helm
DOI
10.1515/bc.2009.096
eISSN
1437-4315
Externe Identifier
  • PubMed Identifier: 19558320
Open access
false
ISSN
1431-6730
Ausgabe der Veröffentlichung
9
Zeitschrift
Biological chemistry
Schlüsselwörter
  • Polyamines
  • tRNA Methyltransferases
  • Electrophoresis
  • Ultraviolet Rays
  • Nucleic Acid Conformation
  • RNA Stability
  • Methylation
  • Transition Temperature
  • Quaternary Ammonium Compounds
Sprache
eng
Medium
Print
Paginierung
851 - 861
Datum der Veröffentlichung
2009
Status
Published
Datum der Datenerfassung
2009
Titel
Effect of a quaternary pentamine on RNA stabilization and enzymatic methylation.
Sub types
  • Journal Article
Ausgabe der Zeitschrift
390

Datenquelle: Europe PubMed Central

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 tRNA(Phe) transcripts by >20 degrees 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 tRNA(Phe). 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 m(2)G/m(2)(2)G by the methyltransferase Trm1p and of m(1)A by TrmIp were not affected or only slightly stimulated by polyamines. In contrast, Taa specifically inhibited Trm4p-dependent formation of m(5)C only in tRNA(Phe), likely by occupying sites that are relevant to RNA recognition by the methyltransferase.
Autoren
  • Armine Hayrapetyan
  • Henri Grosjean
  • Mark Helm
Autoren-URL
https://www.ncbi.nlm.nih.gov/pubmed/19558320
DOI
10.1515/BC.2009.096
eISSN
1437-4315
Ausgabe der Veröffentlichung
9
Zeitschrift
Biol Chem
Schlüsselwörter
  • Electrophoresis
  • Methylation
  • Nucleic Acid Conformation
  • Polyamines
  • Quaternary Ammonium Compounds
  • RNA Stability
  • Transition Temperature
  • Ultraviolet Rays
  • tRNA Methyltransferases
Sprache
eng
Country
Germany
Paginierung
851 - 861
Datum der Veröffentlichung
2009
Status
Published
Datum, an dem der Datensatz öffentlich gemacht wurde
2009
Titel
Effect of a quaternary pentamine on RNA stabilization and enzymatic methylation.
Sub types
  • Journal Article
Ausgabe der Zeitschrift
390

Datenquelle: PubMed

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