The StpA Protein Functions as a Molecular Adapter To Mediate Repression of the bgl Operon by Truncated H-NS in Escherichia coli
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چکیده
منابع مشابه
The StpA protein functions as a molecular adapter to mediate repression of the bgl operon by truncated H-NS in Escherichia coli.
The mechanism of repression of the beta-glucoside utilization (bgl) operon of Escherichia coli by a carboxy-terminally truncated derivative of the nucleoid-associated protein H-NS which is defective in DNA binding was investigated. The DNA-binding function of the H-NS-like protein StpA was found to be necessary for repression, which is consistent with a role for StpA as a DNA-binding adapter fo...
متن کاملBglJ-RcsB heterodimers relieve repression of the Escherichia coli bgl operon by H-NS.
RcsB is the response regulator of the complex Rcs two-component system, which senses perturbations in the outer membrane and peptidoglycan layer. BglJ is a transcriptional regulator whose constitutive expression causes activation of the H-NS- and StpA-repressed bgl (aryl-β,D-glucoside) operon in Escherichia coli. RcsB and BglJ both belong to the LuxR-type family of transcriptional regulators wi...
متن کاملModeling feedback loops in the H-NS-mediated regulation of the Escherichia coli bgl operon.
The histone-like nucleoid-associated protein H-NS is a global transcriptional repressor that controls approximately 5% of all genes in Escherichia coli and other enterobacteria. H-NS binds to DNA with low specificity. Nonetheless, repression of some loci is exceptionally specific. Experimental data for the E. coli bgl operon suggest that highly specific repression is caused by regulatory feedba...
متن کاملFate of the H-NS–Repressed bgl Operon in Evolution of Escherichia coli
In the enterobacterial species Escherichia coli and Salmonella enterica, expression of horizontally acquired genes with a higher than average AT content is repressed by the nucleoid-associated protein H-NS. A classical example of an H-NS-repressed locus is the bgl (aryl-beta,D-glucoside) operon of E. coli. This locus is "cryptic," as no laboratory growth conditions are known to relieve repressi...
متن کاملDifferential dependence of StpA on H-NS in autoregulation of stpA and in regulation of bgl.
StpA has functional similarity to its homologue, the nucleoid structuring protein H-NS. It binds to AT-rich, planar, bent DNA and constrains DNA supercoils. In addition, StpA acts as an RNA chaperone. StpA and H-NS also form heterodimers. However, cellular levels of StpA are low due to repression of stpA by H-NS and negative autoregulation. Here we show that effective (30-fold) repression of st...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1998
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.180.4.994-997.1998