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Conformational flexibility in the enterovirus RNA replication platform

  1. Steven M. Pascal1
  1. 1Department of Chemistry and Biochemistry, Old Dominion University, Norfolk, Virginia 23529, USA
  2. 2Department of Biochemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, USA
  3. 3National Magnetic Resonance Facility at Madison (NMRFAM), University of Wisconsin-Madison, Madison, Wisconsin 53706, USA
  1. Corresponding author: spascal{at}odu.edu
  • 4 Present address: Department of Biochemistry and Biophysics, University of California-San Francisco, San Francisco, California 94143, USA

Abstract

A presumed RNA cloverleaf (5′CL), located at the 5′-most end of the noncoding region of the enterovirus genome, is the primary established site for initiation of genomic replication. Stem–loop B (SLB) and stem–loop D (SLD), the two largest stem–loops within the 5′CL, serve as recognition sites for protein interactions that are essential for replication. Here we present the solution structure of rhinovirus serotype 14 5′CL using a combination of nuclear magnetic resonance spectroscopy and small-angle X-ray scattering. In the absence of magnesium, the structure adopts an open, somewhat extended conformation. In the presence of magnesium, the structure compacts, bringing SLB and SLD into close contact, a geometry that creates an extensive accessible major groove surface, and permits interaction between the proteins that target each stem–loop.

Keywords

  • Received November 1, 2018.
  • Accepted December 19, 2018.

This article is distributed exclusively by the RNA Society for the first 12 months after the full-issue publication date (see http://rnajournal.cshlp.org/site/misc/terms.xhtml). After 12 months, it is available under a Creative Commons License (Attribution-NonCommercial 4.0 International), as described at http://creativecommons.org/licenses/by-nc/4.0/.

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