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Uncoiling c-Jun coiled coils: inhibitory effects of truncated Fos peptides on Jun dimerization and DNA binding in vitro.

Authors
  • Yao, S
  • Brickner, M
  • Pares-Matos, E I
  • Chmielewski, J
Type
Published Article
Journal
Biopolymers
Publication Date
Jan 01, 1998
Volume
47
Issue
4
Pages
277–283
Identifiers
PMID: 10036969
Source
Medline
License
Unknown

Abstract

c-Jun is an oncoprotein that comprises a portion of the AP-1 transcription factor and belongs to the basic-leucine zipper (bZIP) DNA binding protein family. Using peptides derived from the leucine zipper region of Fos, we have developed agents that inhibit Jun's DNA binding in the low micromolar range. Fos peptides that were effective inhibitors in the DNA binding assay were also found to inhibit cellular Jun binding to an AP-1 site in a luciferase reporter plasmid in MCF-7 cells. Size exclusion studies confirmed that peptides that inhibit the DNA binding of Jun also inhibit its dimerization. These peptides were found to have a cytotoxic effect on the MCF-7 cell line when delivered with the transfecting agent Tfx-50, possibly due to their role as transcription factor regulators.

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