Single-Molecule FRET Studies of Counterion Effects on the Free Energy Landscape of Human Mitochondrial Lysine tRNA

Publikationstyp:
Zeitschriftenaufsatz
Metadaten:
Autoren
  • Kirsten Dammertz
  • Martin Hengesbach
  • Mark Helm
  • G Ulrich Nienhaus
  • Andrei Yu Kobitski
Autoren-URL
https://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=fis-test-1&SrcAuth=WosAPI&KeyUT=WOS:000289319700007&DestLinkType=FullRecord&DestApp=WOS_CPL
DOI
10.1021/bi101804t
Externe Identifier
  • Clarivate Analytics Document Solution ID: 747KW
  • PubMed Identifier: 21375355
ISSN
0006-2960
Ausgabe der Veröffentlichung
15
Zeitschrift
BIOCHEMISTRY
Paginierung
3107 - 3115
Datum der Veröffentlichung
2011
Status
Published
Titel
Single-Molecule FRET Studies of Counterion Effects on the Free Energy Landscape of Human Mitochondrial Lysine tRNA
Sub types
  • Article
Ausgabe der Zeitschrift
50

Datenquelle: Web of Science (Lite)

Andere Metadatenquellen:
Autoren
  • Kirsten Dammertz
  • Martin Hengesbach
  • Mark Helm
  • G Ulrich Nienhaus
  • Andrei Yu Kobitski
DOI
10.1021/bi101804t
eISSN
1520-4995
ISSN
0006-2960
Ausgabe der Veröffentlichung
15
Zeitschrift
Biochemistry
Sprache
en
Online publication date
2011
Paginierung
3107 - 3115
Datum der Veröffentlichung
2011
Status
Published
Herausgeber
American Chemical Society (ACS)
Herausgeber URL
http://dx.doi.org/10.1021/bi101804t
Datum der Datenerfassung
2023
Titel
Single-Molecule FRET Studies of Counterion Effects on the Free Energy Landscape of Human Mitochondrial Lysine tRNA
Ausgabe der Zeitschrift
50

Datenquelle: Crossref

Abstract
The folding energy landscape of RNA is greatly affected by interactions between the RNA and counterions that neutralize the backbone negative charges and may also participate in tertiary contacts. Valence, size, coordination number, and electron shell structure can all contribute to the energetic stabilization of specific RNA conformations. Using single-molecule fluorescence resonance energy transfer (smFRET), we have examined the folding properties of the RNA transcript of human mitochondrial tRNA(Lys), which possesses two different folded states in addition to the unfolded one under conditions of thermodynamic equilibrium. We have quantitatively analyzed the degree of RNA tertiary structure stabilization for different types of cations based on a thermodynamic model that accounts for multiple conformational states and RNA-ion interactions within each state. We have observed that small monovalent ions stabilize the tRNA tertiary structure more efficiently than larger ones. More ions were found in close vicinity of compact RNA structures, independent of the type of ion. The largest conformation-dependent binding specificity of ions of the same charge was found for divalent ions, for which the ionic radii and coordination properties were responsible for shaping the folding free energy.
Addresses
  • Institute of Biophysics, University of Ulm, 89069 Ulm, Germany.
Autoren
  • Kirsten Dammertz
  • Martin Hengesbach
  • Mark Helm
  • G Ulrich Nienhaus
  • Andrei Yu Kobitski
DOI
10.1021/bi101804t
eISSN
1520-4995
Externe Identifier
  • PubMed Identifier: 21375355
Open access
false
ISSN
0006-2960
Ausgabe der Veröffentlichung
15
Zeitschrift
Biochemistry
Schlüsselwörter
  • Humans
  • Cations
  • RNA
  • RNA, Messenger
  • RNA, Transfer, Lys
  • Fluorescence Resonance Energy Transfer
  • Nucleic Acid Conformation
  • RNA Stability
  • Thermodynamics
  • RNA, Mitochondrial
Sprache
eng
Medium
Print-Electronic
Online publication date
2011
Paginierung
3107 - 3115
Datum der Veröffentlichung
2011
Status
Published
Datum der Datenerfassung
2011
Titel
Single-molecule FRET studies of counterion effects on the free energy landscape of human mitochondrial lysine tRNA.
Sub types
  • Research Support, Non-U.S. Gov't
  • Journal Article
Ausgabe der Zeitschrift
50

Datenquelle: Europe PubMed Central

Abstract
The folding energy landscape of RNA is greatly affected by interactions between the RNA and counterions that neutralize the backbone negative charges and may also participate in tertiary contacts. Valence, size, coordination number, and electron shell structure can all contribute to the energetic stabilization of specific RNA conformations. Using single-molecule fluorescence resonance energy transfer (smFRET), we have examined the folding properties of the RNA transcript of human mitochondrial tRNA(Lys), which possesses two different folded states in addition to the unfolded one under conditions of thermodynamic equilibrium. We have quantitatively analyzed the degree of RNA tertiary structure stabilization for different types of cations based on a thermodynamic model that accounts for multiple conformational states and RNA-ion interactions within each state. We have observed that small monovalent ions stabilize the tRNA tertiary structure more efficiently than larger ones. More ions were found in close vicinity of compact RNA structures, independent of the type of ion. The largest conformation-dependent binding specificity of ions of the same charge was found for divalent ions, for which the ionic radii and coordination properties were responsible for shaping the folding free energy.
Autoren
  • Kirsten Dammertz
  • Martin Hengesbach
  • Mark Helm
  • G Ulrich Nienhaus
  • Andrei Yu Kobitski
Autoren-URL
https://www.ncbi.nlm.nih.gov/pubmed/21375355
DOI
10.1021/bi101804t
eISSN
1520-4995
Ausgabe der Veröffentlichung
15
Zeitschrift
Biochemistry
Schlüsselwörter
  • Cations
  • Fluorescence Resonance Energy Transfer
  • Humans
  • Nucleic Acid Conformation
  • RNA
  • RNA Stability
  • RNA, Messenger
  • RNA, Mitochondrial
  • RNA, Transfer, Lys
  • Thermodynamics
Sprache
eng
Country
United States
Paginierung
3107 - 3115
Datum der Veröffentlichung
2011
Status
Published
Datum, an dem der Datensatz öffentlich gemacht wurde
2011
Titel
Single-molecule FRET studies of counterion effects on the free energy landscape of human mitochondrial lysine tRNA.
Sub types
  • Journal Article
  • Research Support, Non-U.S. Gov't
Ausgabe der Zeitschrift
50

Datenquelle: PubMed

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