Fos leucine zipper variants with increased association capacity.

doi:10.1074/jbc.270.39.22721

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Back to search

Article

Fos leucine zipper variants with increased association capacity.

The Journal of biological chemistry - 29 Sept 1995

Porte D, Oertel-Buchheit P, Granger-Schnarr M, Schnarr M

Abstract excerpt

The Fos wild-type leucine zipper is unable to support homodimerization. This finding is generally explained by the negative net charge of the Fos zipper leading to the electrostatic repulsion of two monomers. Using a LexA-dependent in vivo assay in Escherichia coli, we show here that additional antideterminants for Fos zipper association are the residues in position a within the Fos zipper interface. If the...

Topics

3T3 Cells
Amino Acid Sequence
Animals
Bacterial Proteins
Base Sequence
Binding Sites
DNA-Binding Proteins
Escherichia coli
Genes, fos
Genetic Variation
Kinetics
Leucine Zippers

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mice

Models, Molecular

Molecular Sequence Data

Mutagenesis, Insertional

Mutagenesis, Site-Directed

Proto-Oncogene Proteins c-fos

Source

Open in PubMed

Identifiers

PMID: 7559397
DOI: 10.1074/jbc.270.39.22721

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7559397-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Fos leucine zipper variants with increased association capacity.PMID 7559397Read ↗

DNA binding and transactivation properties of Fos variants with homodimerization capacity.Semantic proximity Read ↗

Non-leucine residues in the leucine repeats of Fos and Jun contribute to the stability and determine the specificity of dimerization.Semantic proximity Read ↗

Buried asparagines determine the dimerization specificities of leucine zipper mutants.Semantic proximity Read ↗

A new LexA-based genetic system for monitoring and analyzing protein heterodimerization in Escherichia coli.Semantic proximity Read ↗

Design of a bZip transcription factor with homo/heterodimer-induced DNA-binding preference.Semantic proximity Read ↗

Both Jun and Fos contribute to transcription activation by the heterodimer.Semantic proximity Read ↗

A novel, transformation-relevant activation domain in Fos proteins.Semantic proximity Read ↗

Accumulated helix-destabilizing mutations in the leucine zipper of c-Fos leads to attenuation and temperature sensitivity of function.Semantic proximity Read ↗

Detection of tetramerization domains in vivo by cooperative DNA binding to tandem lambda operator sites.Semantic proximity Read ↗

Sequence requirements for coiled-coils: analysis with lambda repressor-GCN4 leucine zipper fusions.Semantic proximity Read ↗

A LexA mutant repressor with a relaxed interdomain linker.Semantic proximity Read ↗

Transformation by FosB requires a trans-activation domain missing in FosB2 that can be substituted by heterologous activation domains.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.