Isolation of a Mutant of Escherichia coli with a Temperature-sensitive Fructose-1,6-Diphosphate Aldolase Activity
- 31 July 1966
- journal article
- research article
- Published by American Society for Microbiology in Journal of Bacteriology
- Vol. 92 (2), 464-+
- https://doi.org/10.1128/jb.92.2.464-469.1966
Abstract
A mutant of E. coli was isolated which was able to grow in rich medium at 30 C but not at 40 C. Upon exposure to 40 C, the cells immediatelystoppedribonucleic-acid (RNA) and deoxyribonucleic-acid synthesis, but protein synthesis continued at a diminished rate for a short time. Addition of chloram-phenicol did not release RNA synthesis from inhibition at 40 C. Synthesis of [beta]-galactosidase could be induced at high temperature despite the presence of glucose in the medium, indicating a lesion in glucose catabolism. Of many catabolic enzymes tested in cell-free extracts, only fructose-l,6-diphosphate aldolase activity appeared to be altered in the mutant cells. No activity was demonstrable in extracts of mutant cells grown at either 30 or 40 C, but determination of glucose-oxidation patterns revealed that the enzyme is probably active in-vivo at 30 C. Temperature-resistant secondary mutants were found to have partially or fully restored aldolase activity, and temperature-resistant recombinants had normal aldolase activity, indicating that the growth pattern and the altered aldolase had a common genetic basis. Linkage data permitted the assignment of an approximate map location for the mutated aldolase gene.This publication has 8 references indexed in Scilit:
- Genetic mapping off fructose-1,6-diphosphatase in Escherichia coliJournal of Bacteriology, 1965
- Protein and Nucleic Acid Synthesis in Two Mutants of Escherichia coli with Temperature-Sensitive Aminoacyl Ribonucleic Acid SynthetasesJournal of Bacteriology, 1965
- The Regulation of RNA Synthesis in BacteriaProgress in Nucleic Acid Research and Molecular Biology, 1964
- Studies on the induction of β-galactosidase in a cryptic strain of Escherichia coliBiochimica et Biophysica Acta, 1959