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PMID: 2974122 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

The role of the leucine zipper in the fos-jun interaction.

Nature ·Vol. 336 ·No. 6200 ·1988-12-15 ·Pages 646-51

Kouzarides T, Ziff E

Abstract

Mutagenesis of the fos protein supports the hypothesis that a heptad repeat of leucine residues stabilizes the interaction between the fos and jun proteins. We show that the complex between fos and jun can bind to DNA more tightly than either protein alone and that basic residues adjacent to the leucine repeat of fos contribute to the DNA-binding potential of the complex.

MeSH Terms

Animals Bacteriophage lambda/metabolism Binding Sites DNA/metabolism DNA-Binding Proteins/genetics,metabolism In Vitro Techniques Leucine/physiology Mutation Oligonucleotides/metabolism Proto-Oncogene Proteins/genetics,metabolism Proto-Oncogene Proteins c-fos Proto-Oncogene Proteins c-jun Proto-Oncogene Proteins c-myc Rabbits Transcription Factors/genetics,metabolism

Chemicals

DNA-Binding Proteins Oligonucleotides Proto-Oncogene Proteins Proto-Oncogene Proteins c-fos Proto-Oncogene Proteins c-jun Proto-Oncogene Proteins c-myc Transcription Factors DNA Leucine

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Kouzarides T

Department of Biochemistry, New York University Medical Center, New York 10016.

Ziff E

Article Info

Journal

Nature

Abbr.

Nature

ISSN

0028-0836

DOI

10.1038/336646a0

Published

1988-12-15

Pages

646-51

Language

English

Region

England

NLM ID

0410462

Subset

External Links

PubMed source DOI: 10.1038/336646a0 View journal details

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The role of the leucine zipper in the fos-jun interaction.

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