Characterization of the CysB protein of Klebsiella aerogenes: direct evidence that N-acetylserine rather than O-acetylserine serves as the inducer of the cysteine regulon
| Autor: | Richard Tyrrell, Anthony J. Wilkinson, Stephen J. Smerdon, G S Briggs, A S Lynch |
|---|---|
| Rok vydání: | 1994 |
| Předmět: |
DNA
Bacterial Salmonella typhimurium Molecular Sequence Data Mutant Biology Enterobacter aerogenes medicine.disease_cause Regulon Biochemistry chemistry.chemical_compound Bacterial Proteins Escherichia coli Serine medicine Amino Acid Sequence Cysteine Cloning Molecular Binding site Molecular Biology Peptide sequence Binding Sites Base Sequence Sequence Homology Amino Acid Cell Biology biology.organism_classification Molecular biology DNA-Binding Proteins Klebsiella pneumoniae chemistry O-Acetylserine Research Article |
| Zdroj: | Scopus-Elsevier |
| ISSN: | 1470-8728 0264-6021 |
| DOI: | 10.1042/bj2990129 |
| Popis: | The cysB gene of Klebsiella aerogenes has been cloned, sequenced and shown to complement the cysteine auxotrophic phenotype of Escherichia coli cysB mutants. The K. aerogenes cysB gene is predicted to encode a protein of 324 amino acid residues that shares approx. 95% sequence similarity with the Salmonella typhimurium and E. coli CysB proteins. Gel-retardation assays demonstrate that the purified protein binds to DNA fragments containing either the K. aerogenes cysb promoter or the S. typhimurium cysJIH promoter. Acetylserine enhances CysB binding to the cysJIH promoter fragment while diminishing its binding to the cysB promoter fragment. Fluorescence-emission-spectroscopy measurements suggest strongly that N-acetylserine binds to CysB apoprotein but that O-acetylserine does not, and support the notion that N-acetylserine is the physiological inducer of cysteine biosynthesis. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|