Acidic-phospholipid deficiency represses the flagellar master operon through a novel regulatory region in Escherichia coli.
The Escherichia coli pgsA3 mutation, which causes acidic-phospholipid deficiency, was found to repress the flagellar master operon, as assessed by the beta-galactosidase activities of flhD-lacZ fusions. This explained the impairment of flagellar formation and motility by the mutation. A series of deletion analysis indicated that a 40-bp region, at the 5' end of the flhD locus examined, was responsible for the repression of a downstream transcription initiation that was catabolite-repression sensitive. This novel regulatory region was 200 bp upstream of the first possible translation initiation site.
Kitamura
E
E
Department of Biochemistry, Saitama University, Urawa, Japan.
Nakayama
Y
Y
Matsuzaki
H
H
Matsumoto
K
K
Shibuya
I
I
D001426:Bacterial Proteins / Q000235:genetics* / Q000378:metabolism; D001483:Base Sequence; D004268:DNA-Binding Proteins / Q000235:genetics* / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics* / Q000378:metabolism; D029968:Escherichia coli Proteins; D008969:Molecular Sequence Data; D009154:Mutation; D009876:Operon; D010743:Phospholipids / Q000378:metabolism*; D012045:Regulatory Sequences, Nucleic Acid; D015534:Trans-Activators / Q000235:genetics* / Q000378:metabolism; D001616:beta-Galactosidase / Q000378:metabolism
D001426:Bacterial Proteins; D004268:DNA-Binding Proteins; D029968:Escherichia coli Proteins; D010743:Phospholipids; D015534:Trans-Activators; C090553:flhD protein, E coli; D001616:beta-Galactosidase