Temperature-sensitive suppressor mutations of the Escherichia coli DNA gyrase B protein
Autor: | S J, Blance, N L, Williams, Z A, Preston, J, Bishara, M S, Smyth, A, Maxwell |
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Rok vydání: | 2000 |
Předmět: |
Models
Molecular Antibiotics Antineoplastic Protein Conformation Glycine Temperature Valine Crystallography X-Ray DNA Topoisomerases Type II Phenotype Suppression Genetic Models Chemical Coumarins DNA Gyrase Drug Resistance Neoplasm Escherichia coli Mutagenesis Site-Directed bacteria Thermodynamics Enzyme Inhibitors Novobiocin Research Article |
Zdroj: | Protein science : a publication of the Protein Society. 9(5) |
ISSN: | 0961-8368 |
Popis: | Escherichia coli strain LE316 contains a mutation in gyrB that results in the substitution of Val164 to Gly and confers both chlorobiocin resistance and temperature sensitivity. Selection for suppressors of the ts phenotype yielded second-site mutations in GyrB at His38 and Thr157. The properties of proteins bearing these mutations have been characterized, and a mechanism of suppression is proposed based upon structural considerations. |
Databáze: | OpenAIRE |
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