Leucine-zipper motif update

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Leucine Zipper

The leucine zipper is the dimerization domain of the B-ZIP (basic-region leucine zipper) class of eukaryotic transcription factors (Vinson et al., 1989). The name arose because leucines occur every seven amino acids in this dimerization domain.These leucines are critical for the dimerization and DNA binding of B-ZIP proteins. The leucine zipper is a left-handed parallel dimeric coiled-coil, a s...

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Leucine Zipper Mutants

Coiled-coil sequences in proteins consist of heptad repeats containing two characteristic hydrophobic positions. The role of these buried hydrophobic residues in determining the structures of coiled coils was investigated by studying mutants of the GCN4 leucine zipper. When sets of buried residues were altered, two-, three-, and four-helix structures were formed. The x-ray crystal structure of ...

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A leucine zipper-like motif and a basic region-leucine zipper-like element in rat ribosomal protein L13a. Identification of the tum- transplantation antigen P198.

The amino acid sequence of the rat 60 S ribosomal subunit protein L13a was deduced from the sequence of nucleotides in two recombinant cDNAs. Mature ribosomal protein L13a has 202 amino acids (the NH2-terminal methionine is removed after translation of the mRNA) and a M(r) of 23,330. Hybridization of the L13a cDNA to digests of nuclear DNA suggests that there are 9-11 copies of the L13a gene. T...

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Redox-dependent oligomerization through a leucine zipper motif is essential for MG53-mediated cell membrane repair.

We recently discovered that MG53, a muscle-specific tripartite motif (TRIM) family protein, functions as a sensor of oxidation to nucleate the assembly of cell membrane repair machinery. Our data showed that disulfide bond formation mediated by Cys242 is critical for MG53-mediated translocation of intracellular vesicles toward the injury sites. Here we test the hypothesis that leucine zipper mo...

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A Conserved Leucine Zipper Motif in Gammaherpesvirus ORF52 Is Critical for Distinct Microtubule Rearrangements

Productive viral infection often depends on the manipulation of the cytoskeleton. Herpesviruses, including rhesus monkey rhadinovirus (RRV) and its close homolog, the oncogenic human gammaherpesvirus Kaposi's sarcoma-associated herpesvirus/human herpesvirus 8 (KSHV/HHV8), exploit microtubule (MT)-based retrograde transport to deliver their genomes to the nucleus. Subsequently, during the lytic ...

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ژورنال

عنوان ژورنال: Nature

سال: 1989

ISSN: 0028-0836,1476-4687

DOI: 10.1038/340103a0