The carboxy terminus of the viral Jun oncoprotein is required for complex formation with the cellular Fos protein.

Abstract:

:The products of the proto-oncogenes c-jun and c-fos are known to form a complex in vivo. Complex formation appears to stabilize protein-DNA interactions and is thought to play an important functional role in transcriptional regulation. Here we show that the viral Jun oncoprotein, which differs structurally from cellular Jun, is also capable of complex formation with Fos. Thus the oncogenic potency of viral Jun is unlikely to be due to an altered affinity for Fos. We have also defined, by deletion analysis, the domain of v-Jun responsible for complex formation to reside in the carboxy terminus encompassing the leucine zipper motif. We find that complex formation with c-Fos does not occur with v-Jun deletions affecting one or more leucine residues in the zipper domain. Our results are consistent with the hypothesis that the leucine zipper mediates Jun-Fos interaction.

journal_name

Oncogene

journal_title

Oncogene

authors

Bos TJ,Rauscher FJ 3rd,Curran T,Vogt PK

subject

Has Abstract

pub_date

1989-02-01 00:00:00

pages

123-6

issue

2

eissn

0950-9232

issn

1476-5594

journal_volume

4

pub_type

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