Mutations in the lacY gene of Escherichia coli define functional organization of lactose permease
| Autor: | D. Buchel, H. Bocklage, Benno Müller-Hill, M. Mieschendahl |
|---|---|
| Rok vydání: | 1981 |
| Předmět: |
Lactose permease
Proton binding Monosaccharide Transport Proteins lac operon Biological Transport Active medicine.disease_cause Substrate Specificity Structure-Activity Relationship medicine Escherichia coli Amino Acid Sequence Gene Genetics Mutation Multidisciplinary Binding Sites biology Base Sequence Symporters Membrane transport protein Point mutation Escherichia coli Proteins Membrane Transport Proteins Biochemistry Lac Operon biology.protein Chromosome Deletion Protons Research Article |
| Zdroj: | Proceedings of the National Academy of Sciences of the United States of America. 78(12) |
| ISSN: | 0027-8424 |
| Popis: | Mutations in the lacY gene of Escherichia coli have been used to analyze the functional organization of lactose permease. Deletions suggest that the NH2 terminus of lactose permease is not essential and can be replaced by residues of the cytoplasmic enzyme beta-galactosidase. Negative dominant mutations in the lacY gene can be explained by the assumption that membrane-associated lactose permease is active as a dimer or oligomer. The map positions of these mutations and other point mutations that lower or alter the sugar specificity define regions of lactose permease involved in sugar or proton binding and transport. |
| Databáze: | OpenAIRE |
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