Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:2.7.7.6 (RNA polymerase)
 34,946 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The P2 promoter of proP, encoding a transporter for proline and glycine betaine in Escherichia coli, is a unique paradigm, where master regulators of different growth stages, Fis and sigma(S) (RpoS), collaborate to achieve promoter activation. It is also the only case described where Fis functions as class II transcriptional activator (centred at -41). Here we show that the degenerate -35 sequence, and the location of the Fis binding site, which forces a suboptimal 16 bp spacing between the -35 and -10 elements, allow only sigma(S) but not sigma(70) to function at proP (P2). Moreover, the interface between Fis and sigma(S) seems better suited to sigma(S), due to a single residue difference between sigma(S) and sigma(70). Nevertheless, Fis can activate RNA polymerase containing sigma(70) at a proP (P2) promoter variant, in which a typical sigma(70)-35 recognition sequence has been introduced at a 17 bp distance from the -10 hexamer. In summary, we elucidate the rules that govern sigma factor selectivity in the presence of a class II activator, provide new insight into transcriptional activation by Fis from this position, and clarify, why the proP (P2) promoter is precisely activated during a short time window of the growth cycle, when Fis and sigma(S) are both present.
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PMID:The -35 sequence location and the Fis-sigma factor interface determine sigmas selectivity of the proP (P2) promoter in Escherichia coli. 1730 3

The busA locus of Lactococcus lactis encodes a glycine betaine uptake system. At low osmolarity, the transcription of busA is repressed by the BusR protein, which is responsible for the osmotic inducibility of the busA promoter (busAp). In this work, we investigated the mechanism of the osmo-dependent repression by BusR. We found that BusR binding to the busA promoter is dependent on the ionic strength in vitro. Using a BusR derivative carrying a phosphorylation site and the Escherichia coli RNA polymerase holoenzyme, we showed that these proteins are able to form a stable ternary complex by both binding to the same busAp fragment. The association/dissociation of BusR to the RNA polymerase-busAp complex is strictly correlated to the surrounding ionic strength. Together, these results suggest that during growth at low osmolarity BusR represses transcription from busAp at a step further the recruitment of the RNA polymerase. At high osmolarity, an elevated cytoplasmic ionic strength would dissociate BusR from busAp, resulting in the osmotic induction of the busA operon.
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PMID:Osmotic regulation of transcription in Lactococcus lactis: ionic strength-dependent binding of the BusR repressor to the busA promoter. 1760 47


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