Characterization of polynucleotide phosphorylase mutants of Escherichia coli.
Three polynucleotide phosphorylase mutations, isolated in heavily mutagenized Escherichia coli strains Q7, Q13, and Q27, were characterized after their transfer by P1 transduction to nearly isogenic strains which lack ribonuclease I. Each strain has a different altered form of polynucleotide phosphorylase. One enzyme exhibited sharply reduced activity under all conditions tested. A second had reduced activity which was stimulated by Mn(++). The third enzyme was thermolabile and could be >95% inactivated in vivo at 44 C and pH 6 if the cells were prevented from growing; during growth under these and other conditions, the full enzyme level was maintained. The strains showed no differences from the wild type in their growth rates, their adjustments to changes in media and temperature, or their recoveries from starvation.
D002499:Centrifugation, Density Gradient; D002852:Chromatography, Ion Exchange; D004586:Electrophoresis; D004926:Escherichia coli / Q000187:drug effects; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D008274:Magnesium / Q000494:pharmacology; D008345:Manganese / Q000494:pharmacology; D009153:Mutagens / Q000494:pharmacology; D009154:Mutation; D009713:Nucleotidyltransferases / Q000378:metabolism; D014161:Transduction, Genetic
D009153:Mutagens; D008345:Manganese; D009713:Nucleotidyltransferases; D008274:Magnesium