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Journal ArticleDOI

The leucine zipper: a hypothetical structure common to a new class of DNA binding proteins

William H. Landschulz, +2 more
- 24 Jun 1988 - 
- Vol. 240, Iss: 4860, pp 1759-1764
TLDR
A 30-amino-acid segment of C/EBP, a newly discovered enhancer binding protein, shares notable sequence similarity with a segment of the cellular Myc transforming protein, and may represent a characteristic property of a new category of DNA binding proteins.
Abstract
A 30-amino-acid segment of C/EBP, a newly discovered enhancer binding protein, shares notable sequence similarity with a segment of the cellular Myc transforming protein. Display of these respective amino acid sequences on an idealized alpha helix revealed a periodic repetition of leucine residues at every seventh position over a distance covering eight helical turns. The periodic array of at least four leucines was also noted in the sequences of the Fos and Jun transforming proteins, as well as that of the yeast gene regulatory protein, GCN4. The polypeptide segments containing these periodic arrays of leucine residues are proposed to exist in an alpha-helical conformation, and the leucine side chains extending from one alpha helix interdigitate with those displayed from a similar alpha helix of a second polypeptide, facilitating dimerization. This hypothetical structure is referred to as the "leucine zipper," and it may represent a characteristic property of a new category of DNA binding proteins.

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Citations
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Journal ArticleDOI

Predicting coiled coils from protein sequences

TL;DR: This method was used to delineate coiled-coil domains in otherwise globular proteins, such as the leucine zipper domains in transcriptional regulators, and to predict regions of discontinuity within coiled -coil structures,such as the hinge region in myosin.
Journal ArticleDOI

Induction of apoptosis in fibroblasts by c-myc protein

TL;DR: It is demonstrated that deregulated c-myc expression induces apoptosis in cells growth arrested by a variety of means and at various points in the cell cycle.
Journal ArticleDOI

Transcriptional regulation in mammalian cells by sequence-specific DNA binding proteins

TL;DR: This review summarizes recent studies that define structural domains for DNA binding and transcriptional activation functions in sequence-specific transcription factors in mammalian DNA binding transcription factors.
References
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Journal ArticleDOI

Repetitive zinc‐binding domains in the protein transcription factor IIIA from Xenopus oocytes.

TL;DR: Analysis of the amino acid sequence reveals nine tandem similar units, each consisting of approximately 30 residues and containing two invariant pairs of cysteines and histidines, the most common ligands for zinc in the 7S particle of Xenopus laevis oocytes, which suggests that the protein contains repetitive zinc‐binding domains.
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Isolation of cDNA encoding transcription factor Sp1 and functional analysis of the DNA binding domain.

TL;DR: It is found that purified Sp1 requires Zn(II) for sequence-specific binding to DNA, and it is likely that Sp1 interacts with DNA by binding of the Zn (II) fingers.
Journal ArticleDOI

Protein-DNA Recognition

TL;DR: The current models for the complexes of Cro, repressor, and CAP with operator DNA are probably fundamentally correct, but it should be emphasized that model building alone, even when coupled with genetic and biochemical studies, cannot be expected to provide a completely reliable "high-resolution" view of the protein-DNA complex.
Journal ArticleDOI

Potential metal-binding domains in nucleic acid binding proteins.

TL;DR: Observations suggest numerous experiments are needed to determine whether metal-binding domains are present in proteins and, if present, what roles such domains play in the processes of nucleic acid binding and gene regulation.
Journal ArticleDOI

Helix stabilization by Glu-...Lys+ salt bridges in short peptides of de novo design

TL;DR: Four alanine-based peptides were designed, synthesized, and tested by circular dichroism for alpha-helix formation in H2O to test for helix stabilization by (Glu-, Lys+) ion pairs or salt bridges (H-bonded ion pairs).
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