An apaH mutation causes AppppA to accumulate and affects motility and catabolite repression in Escherichia coli.
apaH- mutants lack the hydrolase responsible for degradation of AppppN dinucleotides in Escherichia coli and show a greater than or equal to 16-fold increase in AppppA under nonstress conditions. These mutants lack detectable activity of sigma F, a factor required for transcription of motility and chemotaxis genes. Expression of the flbB/flaI operon, thought to encode sigma F, is decreased in apaH- mutants, and there appears to be a general decrease in expression of genes regulated by cAMP-binding protein and cAMP as well.
Farr
S B
SB
Department of Biochemistry, University of California, Berkeley 94720.
Arnosti
D N
DN
Chamberlin
M J
MJ
Ames
B N
BN
D002465:Cell Movement; D004251:DNA Transposable Elements; D015226:Dinucleoside Phosphates / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics* / Q000378:metabolism / Q000502:physiology; D005408:Flagellin / Q000235:genetics; D005686:Galactokinase / Q000235:genetics / Q000378:metabolism; D005796:Genes; D005798:Genes, Bacterial; D005838:Genotype; D006867:Hydrolases / Q000235:genetics*; D009154:Mutation; D009711:Nucleotides / Q000378:metabolism; D014158:Transcription, Genetic; D001616:beta-Galactosidase / Q000235:genetics / Q000378:metabolism
D004251:DNA Transposable Elements; D015226:Dinucleoside Phosphates; D009711:Nucleotides; D005408:Flagellin; C020733:diadenosine tetraphosphate; D005686:Galactokinase; D006867:Hydrolases; D001616:beta-Galactosidase