Binding of U1A protein changes RNA dynamics as observed by 13C NMR relaxation studies.

Binding of U1A protein changes RNA dynamics as observed by 13C NMR relaxation studies. Research Abstract Details 

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Binding of U1A protein changes RNA dynamics as observed by 13C NMR relaxation studies. Abstract Text:

Zahra Shajani,Gary Drobny,Gabriele Varani,

Recognition of RNA by proteins and small molecules often involves large changes in RNA structure and dynamics, yet very few studies have so far characterized these motional changes. Here we extend to the protein-bound RNA recent 13C relaxation studies of motions in the RNA recognized by human U1A protein, a well-known model for protein-RNA recognition. Changes in relaxation observed upon complex formation demonstrate that the protein-binding site becomes rigid in the complex, but the upper stem-loop that defines the secondary structure of this RNA experiences unexpected motional freedom. By using a helix elongation strategy, we observe that the upper stem-loop moves independently of the remainder of the structure also in the absence of U1A. Surprisingly, RNA residues making important intermolecular contacts in the structure of the complex exhibit increased flexibility in the presence of the protein. Both of these results support the hypothesis that RNA-binding proteins select a structure that optimizes intermolecular contacts in the manifold of conformations sampled by the free RNA and that protein binding quenches these motions. Together with previous studies of the RNA-bound protein, they also demonstrate that protein-RNA interfaces experience complex motions that modulate the strength of individual interactions.

Binding of U1A protein changes RNA dynamics as observed by 13C NMR relaxation studies. Publishing Authors By Initials

Z Shajani,G Drobny,G Varani,

For similar natural sciences: physics: thermodynamics research abstracts see: natural sciences: physics: thermodynamics research

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Binding of U1A protein changes RNA dynamics as observed by 13C NMR relaxation studies. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Extr

Journal: Biochemistry

VOLUME: 46

Page Numbers: 5875-83

Journal Abbreviation: Biochemistry

ISSN: 0006-2960

DAY: 1

MONTH: 05

YEAR: 2007

Binding of U1A protein changes RNA dynamics as observed by 13C NMR relaxation studies. Information

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LANGUAGE: eng

NlmUniqueID: 370623

Binding of U1A protein changes RNA dynamics as observed by 13C NMR relaxation studies. Keywords Mesh Terms:

KEYWORDS: Thermodynamics

MESH TERMS: metabolism

Chemical & Substance for Abstract: Binding of U1A protein changes RNA dynamics as observed by 13C NMR relaxation studies. Information

Substance Name: RNA

Registry Number: 63231-63-0

Grant and Affiliation Information for Binding of U1A protein changes RNA dynamics as observed by 13C NMR relaxation studies.

AFFILIATION: Department of Chemistry, University of Washington, Seattle, Washington 98195-1700, USA.

Country: United States

AGENCY: United States NIBIB

GRANT: EB003152

ACRONYM: EB

MEDLINETA: Biochemistry

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