Isolation and characterization of an Escherichia coli mutant deficient in dTMP kinase activity.
Isolation and characterization of an Escherichia coli mutant deficient in dTMP kinase activity.
复制标题
dTMP 激酶活性缺陷的大肠杆菌突变体的分离和表征。
DOI：
10.1128/jb.157.2.440-444.1984
复制
发表时间：
1984
影响因子：
3.2
通讯作者：
Fuchs,JA
中科院分区：
文献类型：
--
作者：
Daws,TD;Fuchs,JA
Escherichia coli LD0181 is sensitive to 15 micrograms of 2',3'-dideoxythymidine per ml. A derivative that was resistant to 40 micrograms of the same chemical per ml at 30 degrees C and that had lost the ability to grow on enriched medium at 42 degrees C was isolated after nitroso-guanidine mutagenesis. This mutant, TD105, produced a dTMP kinase with 25-fold lower specific activity and a 5-fold higher Km for dTMP than the parental strain. The dTMP pool in TD105 was 4.4-fold higher than in the parent. In addition to temperature sensitivity and resistance to 2',3'-dideoxythymidine, the mutant exhibited a hypersensitivity to 5-bromo-2'-deoxyuridine. All three of these phenotypes are cotransducible. The tmk gene was mapped by cotransduction to approximately 30 min on the E. coli map.
