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The tyranny of adenosine recognition among RNA aptamers to coenzyme A
Authors:Dayal?Saran,Joseph?Frank,Donald?H?Burke  mailto:dhburke@indiana.edu"   title="  dhburke@indiana.edu"   itemprop="  email"   data-track="  click"   data-track-action="  Email author"   data-track-label="  "  >Email author
Affiliation:(1) Department of Chemistry, Indiana University, Bloomington, IN 47405-7102, USA
Abstract:

Background  

Understanding the diversity of interactions between RNA aptamers and nucleotide cofactors promises both to facilitate the design of new RNA enzymes that utilize these cofactors and to constrain models of RNA World evolution. In previous work, we isolated six pools of high affinity RNA aptamers to coenzyme A (CoA), the principle cofactor in biological acyltransfer reactions. Interpretation of the evolutionary significance of those results was made difficult by the fact that the affinity resin attachment strongly influenced the outcome of those selections. Here we describe the selection of four new pools isolated on a disulfide-linked CoA affinity matrix to minimize context-dependent recognition imposed by the attachment to the solid support.
Keywords:
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