Fos-Jun interaction: mutational analysis of the leucine zipper domain of both proteins.

Abstract:

:Jun and Fos oncoproteins form a complex that regulates transcription from promoters containing AP-1 binding sites. The 'leucine zipper' domain of both Fos and Jun is necessary for the formation of the heterodimer, but the role of specific leucine residues is unclear. We have used site-specific mutagenesis to examine the contribution of individual leucine residues to the formation of a stable Fos-Jun protein complex and the binding of this complex to the AP-1 site. Mutation of a single leucine in either Fos or Jun had no effect on protein complex formation. Furthermore, mutations of two consecutive leucines in Jun did not interfere with heterodimer formation; however, in the case of Fos, two consecutive mutations resulted in an inability to form a heterodimer. Although mutagenesis of the first leucine of the heptad repeat had no effect on protein complex formation, this mutation in either Fos or Jun drastically reduced the affinity of the complex for DNA. Thus, both Fos and Jun contribute directly to the DNA-binding potential of the heterodimer.

journal_name

Genes Dev

journal_title

Genes & development

authors

Ransone LJ,Visvader J,Sassone-Corsi P,Verma IM

doi

10.1101/gad.3.6.770

subject

Has Abstract

pub_date

1989-06-01 00:00:00

pages

770-81

issue

6

eissn

0890-9369

issn

1549-5477

journal_volume

3

pub_type

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