A Genetic Screen to Identify Sequences That Mediate Protein Oligomerization in Escherichia coli
| Autor: | Roberto Jappelli, Sydney Brenner |
|---|---|
| Rok vydání: | 1999 |
| Předmět: |
Recombinant Fusion Proteins
Molecular Sequence Data Biophysics Repressor Computational biology medicine.disease_cause Biochemistry Bacteriophage Open Reading Frames Viral Proteins Bacterial Proteins Peptide Library Escherichia coli medicine Protein oligomerization Viral Regulatory and Accessory Proteins Genomic library Amino Acid Sequence Cloning Molecular Molecular Biology Sequence Deletion Genetics biology Reproducibility of Results Cell Biology Protein engineering biology.organism_classification Bacteriophage lambda DNA-Binding Proteins Repressor Proteins Open reading frame Phenotype GATAD2B Peptides Dimerization Protein Binding |
| Zdroj: | Biochemical and Biophysical Research Communications. 266:243-247 |
| ISSN: | 0006-291X |
| Popis: | Many proteins assemble as oligomeric complexes and in several cases a distinct domain mediates the interaction between the subunits. The identification of new oligomerization modules is relevant to comprehend both the architecture and the evolution of protein sequences and also for protein engineering applications. Using the bacteriophage λ repressor dimerization assay, we searched Escherichia coli genomic libraries for sequences able to mediate protein oligomerization in vivo. We identified short peptides that can substitute very effectively the dimerizing domain of the repressor. Most of these peptides belong to open reading frames that are normally not expressed in the bacterial cell. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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