Science (American Association for the Advancement of Science), 1990-12, Vol.250 (4986), p.1400-1403
1990
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Details
- Autor(en) / Beteiligte
- Titel
- Sequence Requirements for Coiled-Coils: Analysis with λ Repressor- GCN4 Leucine Zipper Fusions
- Ist Teil von
- Science (American Association for the Advancement of Science), 1990-12, Vol.250 (4986), p.1400-1403
- Ort / Verlag
- Washington, DC: American Society for the Advancement of Science
- Erscheinungsjahr
- 1990
- Quelle
- MEDLINE
- Beschreibungen/Notizen
- A genetic system was developed in Escherichia coli to study leucine zippers with the amino-terminal domain of bacteriophage λ repressor as a reporter for dimerization. This system was used to analyze the importance of the amino acid side chains at eight positions that form the hydrophobic interface of the leucine zipper dimer from the yeast transcriptional activator, GCN4. When single amino acid substitutions were analyzed, most functional variants contained hydrophobic residues at the dimer interface, while most nonfunctional sequence variants contained strongly polar or helix-breaking residues. In multiple randomization experiments, however, many combinations of hydrophobic residues were found to be nonfunctional, and leucines in the heptad repeat were shown to have a special function in leucine zipper dimerization.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 0036-8075eISSN: 1095-9203DOI: 10.1126/science.2147779Titel-ID: cdi_proquest_miscellaneous_743473406
- Format
- –
- Schlagworte
- Amino Acid Sequence, Amino acid sequencing, Amino acids, Analysis, Bacteriophage lambda - genetics, Bacteriophages, Biochemistry, Biological and medical sciences, Dichroism, Dimerization, Dimers, DNA binding proteins, DNA-Binding Proteins - genetics, Escherichia coli - genetics, Fundamental and applied biological sciences. Psychology, Fungal Proteins - genetics, Genetic Variation, Genetics, Leucine Zippers - genetics, Models, Molecular, Molecular and cellular biology, Molecular genetics, Molecular Sequence Data, Molecular structure, Mutagenesis, Site-Directed, Phenotype, Protein Conformation, Protein Kinases, Proteins, Random Allocation, Recombinant Fusion Proteins - metabolism, Saccharomyces cerevisiae Proteins, Special functions, Superinfection, Transcription Factors - genetics, Transcription. Transcription factor. Splicing. Rna processing, Yeasts