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Uncoiling c-Jun coiled coils: Inhibitory effects of truncated Fos peptides on Jun dimerization and DNA binding in vitro by Shao Yao; Michelle Brickner; Elsie I. Pares-Matos; Jean Chmielewski is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is Uncoiling c-Jun coiled coils: Inhibitory effects of truncated Fos peptides on Jun dimerization and DNA binding in vitro about?

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.

Who reads Uncoiling c-Jun coiled coils: Inhibitory effects of truncated Fos peptides on Jun dimerization and DNA binding in vitro?

Author

Shao Yao; Michelle Brickner; Elsie I. Pares-Matos; Jean Chmielewski

Publisher

Wiley (John Wiley & Sons); John Wiley & Sons Inc.; Wiley (ISSN 0006-3525)

Published

1998

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)