BglJ-RcsB Heterodimers Relieve Repression of the<i>Escherichia coli bgl</i>Operon by H-NS

Venkatesh, Govindarajulu; Koungni, Frant Carlot Kembou; Paukner, Andreas; Stratmann, Thomas; Blissenbach, Birgit; Schnetz, Karin

doi:10.1128/jb.00807-10

Cited by 68 publications

(93 citation statements)

References 62 publications

(85 reference statements)

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“…GadE-RcsB activates expression of the gadA gene, encoding a glutamate decarboxylase important in the acidstress response, whereas phosphorylated RcsB represses expression of gadA as a homodimer by binding to a different site (8). BglJ-RcsB activates expression of Ͼ10 loci, including leuO encoding a pleiotropic LysR-type transcription regulator (9,17,18).…”

mentioning

confidence: 99%

“…RcsB and its auxiliary partners all belong to the FixJ/NarL family of transcriptional regulators characterized by a conserved C-terminal DNA-binding domain family (3,10,11). The interaction of RcsB with the auxiliary partners alters the DNA binding specificity (8,9,12) and thus extends the regulatory repertoire of the Rcs system to the control of multiple loci related to motility and biofilm formation, various stress responses, cell surface components, and additional functions (3,4). As a homodimer, RcsB activates or represses transcription of several loci, including rprA, encoding the small regulatory RNA RprA (3,13).…”

mentioning

confidence: 99%

“…RcsB is a transcriptional regulator that acts as a homodimer or by interaction with auxiliary transcriptional regulators, including RcsA, GadE, and BglJ (3,8,9). RcsB and its auxiliary partners all belong to the FixJ/NarL family of transcriptional regulators characterized by a conserved C-terminal DNA-binding domain family (3,10,11).…”

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confidence: 99%

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Interaction of the RcsB Response Regulator with Auxiliary Transcription Regulators in Escherichia coli

Pannen

Fabisch

Gausling

et al. 2016

Journal of Biological Chemistry

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The Rcs phosphorelay is a two-component signal transduction system that is induced by cell envelope stress. RcsB, the response regulator of this signaling system, is a pleiotropic transcription regulator, which is involved in the control of various stress responses, cell division, motility, and biofilm formation. RcsB regulates transcription either as a homodimer or together with auxiliary regulators, such as RcsA, BglJ, and GadE in Escherichia coli. In this study, we show that RcsB in addition forms heterodimers with MatA (also known as EcpR) and with DctR. Our data suggest that the MatA-dependent transcription regulation is mediated by the MatA-RcsB heterodimer and is independent of RcsB phosphorylation. Furthermore, we analyzed the relevance of amino acid residues of the active quintet of conserved residues, and of surface-exposed residues for activity of RcsB. The data suggest that the activity of the phosphorylation-dependent dimers, such as RcsA-RcsB and RcsB-RcsB, is affected by mutation of residues in the vicinity of the phosphorylation site, suggesting that a phosphorylation-induced structural change modulates their activity. In contrast, the phosphorylation-independent heterodimers BglJ-RcsB and MatA-RcsB are affected by only very few mutations. Heterodimerization of RcsB with various auxiliary regulators and their differential dependence on phosphorylation add an additional level of control to the Rcs system that is operating at the output level.

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Interaction of the RcsB Response Regulator with Auxiliary Transcription Regulators in Escherichia coli

Pannen

Fabisch

Gausling

et al. 2016

Journal of Biological Chemistry

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“…The dimerization interface within the receiver domains is also perfectly conserved between the two proteins, suggesting that they may form heterodimers. Evolutionarily, duplication is thought to be one route that allowed the expansion of two-component systems within bacteria (Capra & Laub, 2012 (Venkatesh et al, 2010). Thus, through heterodimer formation, GvrC may titrate away GvrA, leading to repression of gas vesicle formation.…”

Section: Discussionmentioning

confidence: 99%

Overproduction of individual gas vesicle proteins perturbs flotation, antibiotic production and cell division in the enterobacterium Serratia sp. ATCC 39006

2016

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“…The bgl operon is subject to multiple levels of regulation at the transcriptional as well as posttranscriptional levels (18). To reevaluate the genetic requirements for activity of BglG, we therefore used a reporter system that allows determination of BglG activity independent of the context of the bgl operon ( Fig.…”

Section: Bglg Requires Ei and Either Phosphorylatable Hpr Or Frub Formentioning

confidence: 99%

Activation of Escherichia coli antiterminator BglG requires its phosphorylation

Rothe

Bahr

Stülke

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

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Transcriptional antiterminator proteins of the BglG family control the expression of enzyme II (EII) carbohydrate transporters of the bacterial phosphotransferase system (PTS). In the PTS, phosphoryl groups are transferred from phosphoenolpyruvate (PEP) via the phosphotransferases enzyme I (EI) and HPr to the EIIs, which phosphorylate their substrates during transport. Activity of the antiterminators is negatively controlled by reversible phosphorylation catalyzed by the cognate EIIs in response to substrate availability and positively controlled by the PTS. For the Escherichia coli BglG antiterminator, two different mechanisms for activation by the PTS were proposed. According to the first model, BglG is activated by HPr-catalyzed phosphorylation at a site distinct from the EIIdependent phosphorylation site. According to the second model, BglG is not activated by phosphorylation, but solely through interaction with EI and HPr, which are localized at the cell pole. Subsequently BglG is released from the cell pole to the cytoplasm as an active dimer. Here we addressed this discrepancy and found that activation of BglG requires phosphorylatable HPr or the HPr homolog FruB in vivo. Further, we uniquely demonstrate that purified BglG protein becomes phosphorylated by FruB as well as by HPr in vitro. Histidine residue 208 in BglG is essential for this phosphorylation. These data suggest that BglG is in fact activated by phosphorylation and that there is no principal difference between the PTS-exerted mechanisms controlling the activities of BglG family proteins in Gram-positive and Gram-negative bacteria.histidine protein | carbon catabolite repression | RNA binding protein | β-glucoside operon | antagonistically acting phosphorylations

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BglJ-RcsB Heterodimers Relieve Repression of theEscherichia coli bglOperon by H-NS

Cited by 68 publications

References 62 publications

Interaction of the RcsB Response Regulator with Auxiliary Transcription Regulators in Escherichia coli

Interaction of the RcsB Response Regulator with Auxiliary Transcription Regulators in Escherichia coli

Overproduction of individual gas vesicle proteins perturbs flotation, antibiotic production and cell division in the enterobacterium Serratia sp. ATCC 39006

Activation of Escherichia coli antiterminator BglG requires its phosphorylation

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