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Cited by 80Protein Structure and DynamicsGenomics and Chromatin DynamicsChemical Synthesis and Analysis

Non-leucine residues in the leucine repeats of Fos and Jun contribute to the stability and determine the specificity of dimerization

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Schuermann, Marcus, Hunter, John B., Hennig, Guido, Müller, Rolf·1991·Nucleic Acids Research
DOI 10.1093/nar/19.4.739PMC PMC333705
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Abstract

Various transcription factors, including C/EBP, GCN4 and members of the Fos, Jun and Myc families have been shown to form highly specific complexes via alpha-helical structures referred to as leucine zippers. Experimental evidence has suggested that dimerization involves the formation of hydrophobic bonds between leucine residues in laterally aligned coiled coil structures. However, the specificity of interaction between leucine zipper proteins is not understood. In this study, we show that amino acids, which are located in positions a, e, and g are instrumental in the formation of Fos/Jun heterodimers, presumably by establishing intermolecular electrostatic and hydrophobic interactions. These residues are highly conserved in proteins of the Fos or Jun families but completely different between Fos and Jun, suggesting that these residues determine the specificity of interaction. This conclusion is supported by the observation that the substitution of amino acids in position a or g in Fos with the corresponding Jun amino acids facilitates the association of two Fos leucine repeats. In addition, we show that a conserved histidine residue, located 7 amino acids (i.e., two alpha-helical turns) C-terminally to the 5th leucine in Fos and Jun, is also important for complex formation.

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  • Altering the amino acids at the e and g positions can be enough to change a leucine zipper's dimerization specificity.

    “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 <i>e</i> and <i>g</i> position mutants (1997) · cites this paper as Schuermann et al., 1991

    In “Determinants of preferential dimer formation” (page unavailable), the paper concludes that substitutions at position g change binding specificity, but says this is only probable for position e. The claim presents the effect of changing residues at e and g as established, whereas the evidence for e is qualified. (LLM, conf=0.83)

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Research works printed but not linked: 2

  1. Ryder.K., Lau,L.F., and Nathans.D. (1988). Proc. Natl. Acad. Sci. USA 85, 1487-1491.
  2. Ryder,K., Lanahan.A., Perez-AIbueme.E., and Nathans.D. (1989) Proc. Natl. Acad. Sci. USA 86, 1500-1503. REFERENCES

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Authors
Schuermann, M., Hunter, J. B., Hennig, G., & Müller, R.
Affiliations
Philipps University of Marburg (DE)
Corresponding author
Müller, Rolf
ORCID
Müller, Rolf
Venue
Nucleic Acids Research
Publisher
Oxford University Press (OUP)
Published
1991
Volume
19
Issue
4
Pages
739-746
ISSN
  • 0305-1048 (ISSN-L)
  • 1362-4962
DOI
10.1093/nar/19.4.739
PMC
PMC333705
OpenAlex
W2007468038
Cited by
80
References
44
Citations by year
2023: 1 · 2016: 2 · 2015: 1 · 2013: 1 · 2012: 2
FWCI
4.23
Type
journal article
Language
en
Open access
Locations
  • Nucleic Acids Research (publishedVersion)
  • Europe PMC (PubMed Central) (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
  • MDC Repository (Max-Delbrueck-Center for Molecular Medicine) (acceptedVersion)
Funders
Deutsche Forschungsgemeinschaft
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, c-Jun, leucine zipper, protein dimerization, Fos-Jun heterodimer, protein stability, amino acid substitutions, hydrophobic interactions, electrostatic interactions, histidine residues, transcription factors, coiled coil
MeSH terms
Amino Acid Sequence, Electrophoresis, Polyacrylamide Gel, Molecular Sequence Data, Mutation, Oncogene Proteins, Viral, Repetitive Sequences, Nucleic Acid, Substrate Specificity, Transcription Factors, Retroviridae Proteins, Oncogenic, Leucine Zippers, Oncogene Protein p65(gag-jun), Oncogene Proteins v-fos

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