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Oligoribonucleotide-based gene-specific transcription inhibitors that target the open complex

L Milne1, D M Perrin, D S Sigman

  • 1Department of Biological Chemistry, School of Medicine, and Molecular Biology Institute, UCLA, Los Angeles, California 90095-1570, USA.

Methods (San Diego, Calif.)
|February 22, 2001
PubMed

Insights

Modified oligoribonucleotides that cannot be extended by RNA polymerase inhibit transcription by binding to the DNA open complex. Phosphorothioate analogs show enhanced binding and inhibition compared to standard oligoribonucleotides.

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • Transcription initiation involves the formation of an open complex, a single-stranded DNA bubble.
  • Oligonucleotides can potentially interfere with biological processes by binding to nucleic acids.

Purpose of the Study:

  • To investigate the potential of modified oligoribonucleotides as inhibitors of transcription.
  • To elucidate the mechanism of inhibition and identify optimal inhibitor characteristics.

Main Methods:

  • Utilized lacUV5/Escherichia coli RNA polymerase and trpEDCBA/E. coli RNA polymerase transcription systems.
  • Employed 1,10-phenanthroline-copper to probe oligonucleotide hybridization and DNA binding.
  • Synthesized and tested phosphodiester and phosphorothioate oligoribonucleotide analogs.

Main Results:

  • Oligoribonucleotides lacking a 3'-OH group inhibit transcription by hybridizing to the DNA template strand within the open complex.
  • Effective inhibitors are pentamers complementary to the DNA template from -5 to +2 relative to the transcription start site.
  • Phosphorothioate analogs exhibit increased binding affinity and enhanced transcription inhibition compared to phosphodiester counterparts.
  • Oligonucleotide hybridization occurs in an antiparallel orientation to the DNA target.

Conclusions:

  • Modified oligoribonucleotides represent a viable strategy for inhibiting transcription.
  • The phosphorothioate backbone enhances the efficacy of these transcription inhibitors.
  • Understanding the precise binding interactions within the open complex is crucial for designing effective inhibitors.

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