Literature DB >> 27930881

Ultraslow Domain Motions in HIV-1 TAR RNA Revealed by Solid-State Deuterium NMR.

Wei Huang1, Prashant S Emani1, Gabriele Varani1, Gary P Drobny1.   

Abstract

Intrinsic motions may allow HIV-1 transactivation response (TAR) RNA to change its conformation to form a functional complex with the Tat protein, which is essential for viral replication. Understanding the dynamic properties of TAR necessitates determining motion on the intermediate nanosecond-to-microsecond time scale. To this end, we performed solid-state deuterium NMR line-shape and T1Z relaxation-time experiments to measure intermediate motions for two uridine residues, U40 and U42, within the lower helix of TAR. We infer global motions at rates of ∼105 s-1 in the lower helix, which are much slower than those in the upper helix (∼106 s-1), indicating that the two helical domains reorient independently of one another in the solid-state sample. These results contribute to the aim of fully describing the properties of functional motions in TAR RNA.

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Year:  2016        PMID: 27930881      PMCID: PMC6785184          DOI: 10.1021/acs.jpcb.6b11041

Source DB:  PubMed          Journal:  J Phys Chem B        ISSN: 1520-5207            Impact factor:   2.991


  35 in total

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8.  Methylphosphonate mapping of phosphate contacts critical for RNA recognition by the human immunodeficiency virus tat and rev proteins.

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10.  Elucidating molecular motion through structural and dynamic filters of energy-minimized conformer ensembles.

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Journal:  J Phys Chem B       Date:  2014-02-11       Impact factor: 2.991

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  4 in total

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