Overproduction of acetate kinase activates the phosphate regulon in the absence of the phoR and phoM functions in Escherichia coli.

doi:10.1128/jb.172.5.2245-2249.1990

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Article

Overproduction of acetate kinase activates the phosphate regulon in the absence of the phoR and phoM functions in Escherichia coli.

Journal of bacteriology - 1 May 1990

Lee T Y, Makino K, Shinagawa H, Nakata A

Abstract excerpt

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...

Topics

Acetate Kinase
Adenosine Triphosphate
Alkaline Phosphatase
Carrier Proteins
Cloning, Molecular
DNA, Bacterial
Escherichia coli
Gene Expression Regulation, Bacterial
Genes, Bacterial
Genes, Regulator

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Genetic Vectors

Genotype

Phosphate-Binding Proteins

Phosphotransferases

Plasmids

Restriction Mapping

Source

Open in PubMed Open full text

Identifiers

PMID: 2158965
DOI: 10.1128/jb.172.5.2245-2249.1990
PMCID: PMC208855

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2158965-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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Overproduction of acetate kinase activates the phosphate regulon in the absence of the phoR and phoM functions in Escherichia coli.PMID 2158965Read ↗

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