PMID:12446648

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Citation

Schneider, BL, Ruback, S, Kiupakis, AK, Kasbarian, H, Pybus, C and Reitzer, L (2002) The Escherichia coli gabDTPC operon: specific gamma-aminobutyrate catabolism and nonspecific induction. J. Bacteriol. 184:6976-86

Abstract

Nitrogen limitation induces the nitrogen-regulated (Ntr) response, which includes proteins that assimilate ammonia and scavenge nitrogen. Nitrogen limitation also induces catabolic pathways that degrade four metabolically related compounds: putrescine, arginine, ornithine, and gamma-aminobutyrate (GABA). We analyzed the structure, function, and regulation of the gab operon, whose products degrade GABA, a proposed intermediate in putrescine catabolism. We showed that the gabDTPC gene cluster constitutes an operon based partially on coregulation of GabT and GabD activities and the polarity of an insertion in gabT on gabC. A DeltagabDT mutant grew normally on all of the nitrogen sources tested except GABA. The unexpected growth with putrescine resulted from specific induction of gab-independent enzymes. Nac was required for gab transcription in vivo and in vitro. Ntr induction did not require GABA, but various nitrogen sources did not induce enzyme activity equally. A gabC (formerly ygaE) mutant grew faster with GABA and had elevated levels of gab operon products, which suggests that GabC is a repressor. GabC is proposed to reduce nitrogen source-specific modulation of expression. Unlike a wild-type strain, a gabC mutant utilized GABA as a carbon source and such growth required sigma(S). Previous studies showing sigma(S)-dependent gab expression in stationary phase involved gabC mutants, which suggests that such expression does not occur in wild-type strains. The seemingly narrow catabolic function of the gab operon is contrasted with the nonspecific (nitrogen source-independent) induction. We propose that the gab operon and the Ntr response itself contribute to putrescine and polyamine homeostasis.

Links

PubMed PMC135471

Keywords

4-Aminobutyrate Transaminase/genetics; 4-Aminobutyrate Transaminase/metabolism; Bacterial Proteins; Base Sequence; Biogenic Polyamines/metabolism; DNA-Binding Proteins/physiology; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins; Molecular Sequence Data; Mutation; Nitrogen/metabolism; Operon/physiology; Oxidoreductases/genetics; Oxidoreductases/metabolism; Repressor Proteins/physiology; Transcription Factors/physiology; gamma-Aminobutyric Acid/metabolism

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