Ultraviolet-sensitive Targets in the Enzyme-synthesizing Apparatus ofEscherichia coli
- 1 April 1967
- journal article
- research article
- Published by American Society for Microbiology in Journal of Bacteriology
- Vol. 93 (4), 1210-+
- https://doi.org/10.1128/jb.93.4.1210-1219.1967
Abstract
Inhibition by ultraviolet light of [beta]-galactosidase and alkaline phosphatase synthesis was investigated in both ultraviolet (UV)-sensitive and UV-resistant (wild-type) Escherichia coli. with the objective of determining the sensitivity of various targets. Kinetics of enzyme formation by unmated bacteria and in mating systems, in which the donor provided the specific genetic material and the recipient the cytoplasm, permit the following conclusions regarding the sensitivity of various targets. Catabolite repression resulting from UV damage causes most of the inhibition of [beta]-galactosidase formation. When it is largely eliminated by a step-down in nutrition, the principal target in UV-sensitive bacteria appears to be the structural gene (lacZ+), but damage to the cytoplasm is also important. Transitory inhibition by inactivation of messenger ribonucleic acid is also observed. In wild-type bacteria, repair reduces the importance of lesions in deoxyribonucleic acid sufficiently that cytoplasmic damage appears to be at least as important. Repair occurs within 10 min, as shown by recovery of enzyme-synthesizing ability. Caffeine and proflavine prevent recovery. Newly mated bacteria respond to irradiation very differently than do unmated bacteria. The [beta]-galac-tosidase or alkaline phosphatase structural gene (lacZ+ or phoP+) is much more inhibited after it is transferred than it is in unmated bacteria. This sensitivity seems to depend on a sensitive state of the injected material, rather than on a different physiological condition of the entire zygote. Irradiation of recipient uvr+ bacteria much more strongly inhibited expression of injected genes than if the F- was uvrs. Studies on mating systems are not very useful for learning about the function of unmated bacteria.This publication has 16 references indexed in Scilit:
- Cyclobutane-Type Pyrimidine Dimers in PolynucleotidesScience, 1966
- A second permease for methyl-thio-β-d-galactoside in Escherichia coliBiochimica et Biophysica Acta (BBA) - General Subjects, 1965
- β-Galactosidase: Inactivation of Its Messenger RNA by Ultraviolet IrradiationScience, 1964
- Inactivation of β-galactosidase induction by ultraviolet lightBiochimica et Biophysica Acta (BBA) - Specialized Section on Nucleic Acids and Related Subjects, 1963
- β-galactosidase formation following decay of 32P in Escherichia coli zygotesJournal of Molecular Biology, 1962
- Ultraviolet light and enzyme synthesisJournal of Molecular Biology, 1962
- Genetic control of repression of alkaline phosphatase in E. coliJournal of Molecular Biology, 1961
- The initial kinetics of enzyme inductionBiochimica et Biophysica Acta, 1961
- Inactivation of enzyme formation by ultraviolet lightBiochimica et Biophysica Acta, 1960
- The genetic control and cytoplasmic expression of “Inducibility” in the synthesis of β-galactosidase by E. coliJournal of Molecular Biology, 1959