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Dissection of the ion-induced folding of the hammerhead ribozyme using 19F NMR.

Hammann, Christian ; Norman, D. G. ; Lilley, D. M. (2001)
Dissection of the ion-induced folding of the hammerhead ribozyme using 19F NMR.
In: Proceedings of the National Academy of Sciences of the United States of America, 98 (10)
Artikel, Bibliographie

Kurzbeschreibung (Abstract)

We have used (19)F NMR to analyze the metal ion-induced folding of the hammerhead ribozyme by selective incorporation of 5fluorouridine. We have studied the chemical shift and linewidths of (19)F resonances of 5-fluorouridine at the 4 and 7 positions in the ribozyme core as a function of added Mg(2+). The data fit well to a simple two-state model whereby the formation of domain 1 is induced by the noncooperative binding of Mg(2+) with an association constant in the range of 100 to 500 M(-1), depending on the concentration of monovalent ions present. The results are in excellent agreement with data reporting on changes in the global shape of the ribozyme. However, the NMR experiments exploit reporters located in the center of the RNA sections undergoing the folding transitions, thereby allowing the assignment of specific nucleotides to the separate stages. The results define the folding pathway at high resolution and provide a time scale for the first transition in the millisecond range.

Typ des Eintrags: Artikel
Erschienen: 2001
Autor(en): Hammann, Christian ; Norman, D. G. ; Lilley, D. M.
Art des Eintrags: Bibliographie
Titel: Dissection of the ion-induced folding of the hammerhead ribozyme using 19F NMR.
Sprache: Englisch
Publikationsjahr: 2001
Titel der Zeitschrift, Zeitung oder Schriftenreihe: Proceedings of the National Academy of Sciences of the United States of America
Jahrgang/Volume einer Zeitschrift: 98
(Heft-)Nummer: 10
Kurzbeschreibung (Abstract):

We have used (19)F NMR to analyze the metal ion-induced folding of the hammerhead ribozyme by selective incorporation of 5fluorouridine. We have studied the chemical shift and linewidths of (19)F resonances of 5-fluorouridine at the 4 and 7 positions in the ribozyme core as a function of added Mg(2+). The data fit well to a simple two-state model whereby the formation of domain 1 is induced by the noncooperative binding of Mg(2+) with an association constant in the range of 100 to 500 M(-1), depending on the concentration of monovalent ions present. The results are in excellent agreement with data reporting on changes in the global shape of the ribozyme. However, the NMR experiments exploit reporters located in the center of the RNA sections undergoing the folding transitions, thereby allowing the assignment of specific nucleotides to the separate stages. The results define the folding pathway at high resolution and provide a time scale for the first transition in the millisecond range.

Fachbereich(e)/-gebiet(e): 10 Fachbereich Biologie
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10 Fachbereich Biologie > Regulatorische RNAs und Ribozyme
Hinterlegungsdatum: 29 Jul 2010 12:15
Letzte Änderung: 05 Mär 2013 09:34
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