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B6db references: 12123465.

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
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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