|
type |
Journal Article |
authors |
Belitsky, B.R.; Sonenshein, A.L. |
title |
GabR, a member of a novel protein family, regulates the utilization of gamma-aminobutyrate in Bacillus subtilis |
journal |
Mol Microbiol |
Activity |
2.6.1.19 |
Family |
2.6.1.19.b |
sel |
selected |
ui |
12123465 |
year |
(2002) |
volume |
45 |
number |
2 |
pages |
569-83 |
| |
abstract |
The Bacillus subtilis ycnG (gabT) and ycnH (gabD) genes were shown to encode gamma-aminobutyrate (GABA) aminotransferase and succinic semi-aldehyde dehydrogenase, respectively, and to form a GABA-inducible operon. Null mutations in gabT, gabD or the divergently transcribed ycnF (gabR) gene blocked the utilization of GABA as sole nitrogen source. GabR proved to be a transcriptional activator of the gabTD operon and a negative autoregulator. The target of GabR action was localized to an 87 bp region that includes both gabR and gabT promoters. GabR is a member of a novel but widespread family of chimeric bacterial proteins that have apparent DNA-binding and aminotransferase domains. Mutations in conserved residues of the putative aminotransferase domain abolished GabR function as a transcriptional activator, but did not affect its activity as a negative autoregulator. |
last changed |
2009/04/30 10:25 |
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