Analysis of the NH2-terminal 83rd amino acid of Escherichia coli GyrA in quinolone-resistance
| Autor: | Minoru Yonezawa, Nobuyuki Matsubara, Yasuo Watanabe, Masahiro Takahata, Hirokazu Narita, Naoko Banzawa |
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| Rok vydání: | 1995 |
| Předmět: |
Immunology
Molecular Sequence Data Biology medicine.disease_cause Transfection Microbiology DNA gyrase Polymerase Chain Reaction Serine Structure-Activity Relationship Plasmid Anti-Infective Agents Virology medicine Escherichia coli Site-directed mutagenesis DNA Primers chemistry.chemical_classification Mutation 4-Quinolones Base Sequence Mutagenesis Drug Resistance Microbial Amino acid DNA Topoisomerases Type II Biochemistry chemistry DNA Gyrase Genes Bacterial Mutagenesis Site-Directed Plasmids |
| Zdroj: | Microbiology and immunology. 39(4) |
| ISSN: | 0385-5600 |
| Popis: | Artificial mutations of Gyrase A protein (GyrA) in Escherichia coli by site-directed mutagenesis were generated to analyze quinolone-resistant mechanisms. By genetic analysis of gyrA genes in a gyrA temperature sensitive (Ts) background, exchange of Ser at the NH2-terminal 83rd position of GyrA to Trp, Leu, Phe, Tyr, Ala, Val, and Ile caused bacterial resistance to the quinolones, while exchange to Gly, Asn, Lys, Arg and Asp did not confer resistance. These results indicate that it is the most important for the 83rd amino acid residue to be hydrophobic in expressing the phenotype of resistance to the quinolones. These findings also suggest that the hydroxyl group of Ser would not play a major role in the quinolone-gyrase interaction and Ser83 would not interact directly with other amino acid residues. |
| Databáze: | OpenAIRE |
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