Overproduction of acetate kinase activates the phosphate regulon in the absence of the phoR and phoM functions in Escherichia coli.
A DNA fragment of Escherichia coli cloned on pBR322 elevated the production of alkaline phosphatase and phosphate-binding protein in a phoR phoM strain. Nucleotide sequence analysis and enzyme assays revealed that the DNA fragment contained the ackA gene, which codes for acetate kinase. A high gene dosage of ackA was needed to induce the production of alkaline phosphatase and phosphate-binding protein in this strain. Overexpression of ackA elevated the intracellular ATP concentration, an effect that might be related to activation of the phosphate regulon in the phoR phoM strain.
Lee
T Y
TY
Department of Experimental Chemotherapy, Osaka University, Japan.
Makino
K
K
Shinagawa
H
H
Nakata
A
A
D000084:Acetate Kinase / Q000235:genetics* / Q000302:isolation & purification; D000255:Adenosine Triphosphate / Q000378:metabolism; D000469:Alkaline Phosphatase / Q000235:genetics*; D002352:Carrier Proteins / Q000235:genetics*; D003001:Cloning, Molecular; D004269:DNA, Bacterial / Q000235:genetics; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics* / Q000378:metabolism; D015964:Gene Expression Regulation, Bacterial; D005798:Genes, Bacterial; D005809:Genes, Regulator; D005822:Genetic Vectors; D005838:Genotype; D028044:Phosphate-Binding Proteins; D010770:Phosphotransferases / Q000235:genetics*; D010957:Plasmids; D015183:Restriction Mapping
D002352:Carrier Proteins; D004269:DNA, Bacterial; D028044:Phosphate-Binding Proteins; D000255:Adenosine Triphosphate; D010770:Phosphotransferases; D000084:Acetate Kinase; D000469:Alkaline Phosphatase