Transcription activation by a PNA-Peptide chimera in a mammalian cell extract

Bo Liu, Ying Han, Anwarul Ferdous, David R. Corey, Thomas Kodadek

Research output: Contribution to journalArticle

31 Scopus citations


Synthetic activators that mimic the ability of native transcription factors to recruit the RNA polymerase holoenzyme to specific promoters could, in principle, be constructed by joining a sequence-specific DNA binding moiety with a molecule able to bind the holoenzyme. We report here that a peptide nucleic acid (PNA)-peptide chimera is capable of activating transcription in vitro in a HeLa nuclear extract. Specifically, a promoter-targeted PNA alone acts as a strong inhibitor of basal transcription in a HeLa nuclear extract, presumably due to structural modification of the promoter. However, the fusion of a Gal80-binding peptide to the PNA, but not control peptides, reactivates transcription. The Gal80-binding peptide was selected solely on the basis of its ability to bind the yeast repressor.

Original languageEnglish (US)
Pages (from-to)909-916
Number of pages8
JournalChemistry and Biology
Issue number10
StatePublished - Oct 2003

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Pharmacology
  • Drug Discovery
  • Clinical Biochemistry

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