Anti-Rex Aptamers as RNA Mimics of the Rex-Binding Element

Abstract

RNA molecules that bind tightly and specifically to a Rex fusion protein have been isolated from a conformationally constrained pool of random sequence RNAs. These RNAs effectively mimic a number of features of the wild-type Rex-binding element (XBE). The aptamers compete with the wild-type Rex-binding element for binding to Rex in vitro. The highest-affinity aptamers can specifically bind the Rex ARM, and do not recognize the functionally analogous Rev protein or its ARM. The anti-Rex aptamers can also functionally substitute for the Rex-binding element in vivo, a result which supports a previously proposed model for mRNA transport in which the viral genome serves as a passive platform for assembling and co-opting the cellular transport apparatus. Characteristic sequence and structural motifs found in some of the anti-Rex aptamers may provide insights into the ability of Rex to bind the Rev-responsive element. Overall, these studies suggest that anti-Rex aptamers may serve as effective RNA decoys of Rex.

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Document Details

Document Type
Technical Report
Publication Date
Jan 01, 1997
Accession Number
ADA332241

Entities

People

  • Andrew D Ellington
  • Maria Zapp
  • Scott Baskerville

Organizations

  • Indiana University

Tags

DTIC Thesaurus Topics

  • Amino Acids
  • Cells
  • Chemical Synthesis
  • Chemistry
  • Gene Expression
  • Hiv Infections
  • Insensitive Explosives
  • Lymphocytes
  • Nucleic Acids
  • Organic Chemistry
  • Peptides
  • Proteins
  • Recognition
  • Tissue Culture
  • Trna
  • Virology
  • Viruses

Fields of Study

  • Biology

Readers

  • Molecular Genetics