Altered regulation of the glnRA operon in a Bacillus subtilis mutant that produces methionine sulfoximine-tolerant glutamine synthetase.
A Bacillus subtilis mutant that produced glutamine synthetase (GS) with altered sensitivity to DL-methionine sulfoximine was isolated. The mutation, designated glnA33, was due to a T.A-to-C.G transition, changing valine to alanine at codon 190 within the active-site C domain. Altered regulation was observed for GS activity and antigen and mRNA levels in a B. subtilis glnA33 strain. The mutant enzyme was 28-fold less sensitive to DL-methionine sulfoximine and had a 13.0-fold-higher Km for hydroxylamine and a 4.8-fold-higher Km for glutamate than wild-type GS did.
Schreier
H J
HJ
Center of Marine Biotechnology, University of Maryland, Baltimore 21202.
Rostkowski
C A
CA
Kellner
E M
EM
D001412:Bacillus subtilis / Q000235:genetics*; D005798:Genes, Bacterial; D005974:Glutamate-Ammonia Ligase / Q000037:antagonists & inhibitors / Q000235:genetics*; D005971:Glutamates / Q000378:metabolism; D007700:Kinetics; D008717:Methionine Sulfoximine / Q000494:pharmacology; D009584:Nitrogen / Q000378:metabolism; D009876:Operon; D015183:Restriction Mapping
D005971:Glutamates; D008717:Methionine Sulfoximine; D005974:Glutamate-Ammonia Ligase; D009584:Nitrogen