Affiliation:
1. Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, Massachusetts 02111
Abstract
ABSTRACT
The complete
Bacillus subtilis
genome contains two genes with the potential to encode glutamate dehydrogenase (GlutDH) enzymes. Mutations in these genes were constructed and characterized. The
rocG
gene proved to encode a major GlutDH whose synthesis was induced in media containing arginine or ornithine or, to a lesser degree, proline and was repressed by glucose. A
rocG
null mutant was impaired in utilization of arginine, ornithine, and proline as nitrogen or carbon sources. The
gudB
gene was expressed under all growth conditions tested but codes for a GlutDH that seemed to be intrinsically inactive. Spontaneous mutations in
gudB
that removed a 9-bp direct repeat within the wild-type
gudB
sequence activated the GudB protein and allowed more-efficient utilization of amino acids of the glutamate family.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
144 articles.
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