Bacillus subtilis gnt repressor mutants that diminish gluconate-binding ability.
The Bacillus subtilis gnt operon is negatively regulated by GntR, which is antagonized by gluconate. Three GntR mutants with diminished gluconate-binding ability were obtained. Two were missense mutants (Met-209 to Ile and Ser-230 to Leu), whereas the third had a deletion of the C-terminal 23 amino acids. The mutant GntR proteins were unable to become properly detached from the gnt operator even in the presence of gluconate.
Yoshida
K
K
Department of Biotechnology, Faculty of Engineering, Fukuyama University, Hiroshima, Japan.
Ohmori
H
H
Miwa
Y
Y
Fujita
Y
Y
D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000235:genetics*; D004268:DNA-Binding Proteins / Q000235:genetics*; D029968:Escherichia coli Proteins; D015964:Gene Expression Regulation, Bacterial; D005942:Gluconates / Q000378:metabolism*; D008969:Molecular Sequence Data; D016296:Mutagenesis; D009875:Operator Regions, Genetic / Q000235:genetics; D011485:Protein Binding; D012097:Repressor Proteins / Q000235:genetics*; D017386:Sequence Homology, Amino Acid; D014157:Transcription Factors
D004268:DNA-Binding Proteins; D029968:Escherichia coli Proteins; D005942:Gluconates; C081598:GntR protein, E coli; D012097:Repressor Proteins; D014157:Transcription Factors; C030691:gluconic acid