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RNA Tertiary Interactions in a Riboswitch Stabilize the Structure of a Kink Turn

The kink turn is a widespread RNA motif that introduces an acute kink into the axis of duplex RNA, typically comprising a bulge followed by a G⋅A and A⋅G pairs. The kinked conformation is stabilized by metal ions, or the binding of proteins including L7Ae. We now demonstrate a third mechanism for th...

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Detalles Bibliográficos
Autores principales: Schroeder, Kersten T., Daldrop, Peter, Lilley, David M.J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Cell Press 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3651934/
https://www.ncbi.nlm.nih.gov/pubmed/21893284
http://dx.doi.org/10.1016/j.str.2011.07.003
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author Schroeder, Kersten T.
Daldrop, Peter
Lilley, David M.J.
author_facet Schroeder, Kersten T.
Daldrop, Peter
Lilley, David M.J.
author_sort Schroeder, Kersten T.
collection PubMed
description The kink turn is a widespread RNA motif that introduces an acute kink into the axis of duplex RNA, typically comprising a bulge followed by a G⋅A and A⋅G pairs. The kinked conformation is stabilized by metal ions, or the binding of proteins including L7Ae. We now demonstrate a third mechanism for the stabilization of k-turn structure, involving tertiary interactions within a larger RNA structure. The SAM-I riboswitch contains an essential standard k-turn sequence that kinks a helix so that its terminal loop can make a long-range interaction. We find that some sequence variations in the k-turn within the riboswitch do not prevent SAM binding, despite preventing the folding of the k-turn in isolation. Furthermore, two crystal structures show that the sequence-variant k-turns are conventionally folded within the riboswitch. This study shows that the folded structure of the k-turn can be stabilized by tertiary interactions within a larger RNA structure.
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spelling pubmed-36519342013-05-13 RNA Tertiary Interactions in a Riboswitch Stabilize the Structure of a Kink Turn Schroeder, Kersten T. Daldrop, Peter Lilley, David M.J. Structure Article The kink turn is a widespread RNA motif that introduces an acute kink into the axis of duplex RNA, typically comprising a bulge followed by a G⋅A and A⋅G pairs. The kinked conformation is stabilized by metal ions, or the binding of proteins including L7Ae. We now demonstrate a third mechanism for the stabilization of k-turn structure, involving tertiary interactions within a larger RNA structure. The SAM-I riboswitch contains an essential standard k-turn sequence that kinks a helix so that its terminal loop can make a long-range interaction. We find that some sequence variations in the k-turn within the riboswitch do not prevent SAM binding, despite preventing the folding of the k-turn in isolation. Furthermore, two crystal structures show that the sequence-variant k-turns are conventionally folded within the riboswitch. This study shows that the folded structure of the k-turn can be stabilized by tertiary interactions within a larger RNA structure. Cell Press 2011-09-07 /pmc/articles/PMC3651934/ /pubmed/21893284 http://dx.doi.org/10.1016/j.str.2011.07.003 Text en © 2011 ELL & Excerpta Medica. https://creativecommons.org/licenses/by/3.0/ Open Access under CC BY 3.0 (https://creativecommons.org/licenses/by/3.0/) license
spellingShingle Article
Schroeder, Kersten T.
Daldrop, Peter
Lilley, David M.J.
RNA Tertiary Interactions in a Riboswitch Stabilize the Structure of a Kink Turn
title RNA Tertiary Interactions in a Riboswitch Stabilize the Structure of a Kink Turn
title_full RNA Tertiary Interactions in a Riboswitch Stabilize the Structure of a Kink Turn
title_fullStr RNA Tertiary Interactions in a Riboswitch Stabilize the Structure of a Kink Turn
title_full_unstemmed RNA Tertiary Interactions in a Riboswitch Stabilize the Structure of a Kink Turn
title_short RNA Tertiary Interactions in a Riboswitch Stabilize the Structure of a Kink Turn
title_sort rna tertiary interactions in a riboswitch stabilize the structure of a kink turn
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3651934/
https://www.ncbi.nlm.nih.gov/pubmed/21893284
http://dx.doi.org/10.1016/j.str.2011.07.003
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