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J. Biol. Chem., Vol. 266, Issue 9, 5991-5999, 03, 1991
VJ Hernandez and H Bremer
Escherichia coli has two enzymes catalyzing the synthesis of guanosine
tetraphosphate (ppGpp), designated ppGpp synthetase I (PSI = RelA) and II
(PSII), whose activities are regulated differently. Until now, the gene for
PSII had not been identified. Here, an E. coli relA1 strain that expresses
lacZ from an rrnB P1 promoter was used to screen mutants with increased
beta-galactosidase activity on 5-bromo-4-chloro-3-indoyl beta-D-galactoside
indicator plates at 30 degrees C. About 15% of the mutants obtained in this
manner had reduced levels of ppGpp at 30 degrees C and no detectable ppGpp
at 43 degrees C. These mutants did not form colonies at 42 degrees C on
minimal medium plates and had elevated ribosome concentrations and higher
growth rates at 30 degrees C. Genetic mapping by phage P1 transduction and
complementation analyses showed that the mutations were located in spoT and
that they were recessive. Specific inhibition of SpoT-dependent ppGpp
degradation activity with picolinic acid showed that two of the mutants
tested were deficient in ppGpp synthesis activity. These results indicate
that spoT is required for PSII activity, suggesting that spoT encodes both
ppGpp degradation and synthesis activities and that these two functions can
be affected independently by mutation.
Escherichia coli ppGpp synthetase II activity requires spoT
Molecular Program, University of Texas, Dallas, Richardson 75083-0688.
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