Mechanism of specificity in the Fos-Jun oncoprotein heterodimer

O'Shea, Erin K.; Rutkowski, Rheba; Kim, Peter S.

doi:10.1016/0092-8674(92)90145-3

Cited by 422Protein Structure and DynamicsGenomics and Chromatin DynamicsChemical Synthesis and Analysis

Mechanism of specificity in the Fos-Jun oncoprotein heterodimer

O'Shea, Erin K., Rutkowski, Rheba, Kim, Peter S.·1992·Cell

DOI 10.1016/0092-8674(92)90145-3

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Abstract

Fos and Jun, the protein products of the nuclear proto-oncogenes c-fos and c-jun, associate preferentially to form a heterodimer that binds to DNA and modulates transcription of a wide variety of genes in response to mitogenic stimuli. Both Fos and Jun contain a single leucine zipper region. Previous studies have shown that the leucine zippers of Fos and Jun are necessary and sufficient to mediate preferential heterodimer formation. The leucine zipper regions from Fos and Jun are also known to fold autonomously, most likely as two-stranded, parallel coiled coils. We show here that 8 amino acids from Fos and from Jun are sufficient to mediate preferential heterodimer formation in a background of the GCN4 leucine zipper sequence. Using pH titration and amino acid replacements, we also show that destabilization of the Fos homodimer by acidic residues provides a major thermodynamic driving force for preferential heterodimer formation.

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“Changing the amino acids at the e and g positions can be sufficient to change the dimerization specificity of a leucine zipper (Schuermann et al., 1991; O'Shea et al., 1992, 1993; Vinson et al., 1993; John et al., 1994; Zhou et al., 1994a, 1994b).”
From Oligomerization properties of GCN4 leucine zipper e and g position mutants (1997) · cites this paper as O'Shea et al., 1992

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Authors: O'Shea, E. K., Rutkowski, R., & Kim, P. S.
Affiliations: Howard Hughes Medical Institute (US)
Massachusetts Institute of Technology (US)
ORCID: Kim, Peter S.
Venue: Cell
Publisher: Elsevier BV
Published: 1992-02
Volume: 68
Issue: 4
Pages: 699-708
ISSN: 0092-8674 (ISSN-L)
DOI: 10.1016/0092-8674(92)90145-3
OpenAlex: W2066101080
Cited by: 422
References: 26
Citations by year: 2026: 1 · 2025: 2 · 2024: 4 · 2023: 3 · 2022: 7 · 2021: 4 · 2020: 3 · 2019: 8 · 2018: 3 · 2017: 9 · 2016: 5 · 2015: 7 · 2014: 7 · 2013: 7 · 2012: 14
FWCI: 13.51
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Cell (publishedVersion)
PubMed (publishedVersion)
Funders: Rita Allen Foundation
Allen Foundation
National Institutes of Health (2r01gm044162-10)
National Institute of General Medical Sciences (GM44162)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chemical Synthesis and Analysis
Keywords: Fos-Jun heterodimer, leucine zipper, c-fos, c-Jun, protein-protein interaction specificity, coiled coil, GCN4 leucine zipper, acidic residues, pH titration, amino acid substitutions, transcriptional regulation, mitogenic signaling
MeSH terms: Amino Acid Sequence, Hydrogen-Ion Concentration, Models, Molecular, Molecular Sequence Data, Protein Conformation, Thermodynamics, Molecular Structure, Leucine Zippers, Proto-Oncogene Proteins c-jun, Proto-Oncogene Proteins c-fos

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Mechanism of specificity in the Fos-Jun oncoprotein heterodimer

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