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 journalArticlepeer-review

32 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


Dive into the research topics of 'Transcription activation by a PNA-Peptide chimera in a mammalian cell extract'. Together they form a unique fingerprint.

Cite this