An evolutionary link between sporulation and prophage induction in the structure of a repressor:anti-repressor complex

Lewis, Richard J.; Brannigan, J.A.; Offen, W.A.; Smith, Issar; Wilkinson, Anthony J.

doi:10.1006/jmbi.1998.2163

Cited by 98 publications

(110 citation statements)

References 31 publications

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“…More specifically, an evolutionary link between a prophage and differentiation in B. subtilis has been described in detail. SinR, a repressor protein which regulates the master controller of sporulation, Spo0A, in B. subtilis is structurally identical to the repressor protein of a Bacillus bacteriophage in the DNA binding domain (36). Moreover, a number of B. subtilis cell wall endolysins (enzymes that mediate autolysis during sporulation) are derived from bacteriophage lytic enzymes (37).…”

Section: Resultsmentioning

confidence: 99%

Cell Death in Pseudomonas aeruginosa Biofilm Development

et al. 2003

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Bacteria growing in biofilms often develop multicellular, three-dimensional structures known as microcolonies. Complex differentiation within biofilms of Pseudomonas aeruginosa occurs, leading to the creation of voids inside microcolonies and to the dispersal of cells from within these voids. However, key developmental processes regulating these events are poorly understood. A normal component of multicellular development is cell death. Here we report that a repeatable pattern of cell death and lysis occurs in biofilms of P. aeruginosa during the normal course of development. Cell death occurred with temporal and spatial organization within biofilms, inside microcolonies, when the biofilms were allowed to develop in continuous-culture flow cells. A subpopulation of viable cells was always observed in these regions. During the onset of biofilm killing and during biofilm development thereafter, a bacteriophage capable of superinfecting and lysing the P. aeruginosa parent strain was detected in the fluid effluent from the biofilm. The bacteriophage implicated in biofilm killing was closely related to the filamentous phage Pf1 and existed as a prophage within the genome of P. aeruginosa. We propose that prophage-mediated cell death is an important mechanism of differentiation inside microcolonies that facilitates dispersal of a subpopulation of surviving cells.

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Section: Resultsmentioning

confidence: 99%

Cell Death in Pseudomonas aeruginosa Biofilm Development

et al. 2003

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“…Both the SinR-SinR interaction and the DNA-binding domains of SinR are believed to be needed for SinR to adhere to its operators (Lewis et al 1996(Lewis et al , 1998). Thus, a simple explanation for the classic filamentous phenotype of certain sinR alleles is that the amino acid substitution mutant proteins are impaired in SinR-SinR interaction or in recognition of the slrR promoter and are therefore defective in repressing slrR (which results in overexpression of slrR), but are not defective in promoting cell chaining.…”

Section: Certain Point Mutations Of Sinr Promote Cell Chainingmentioning

confidence: 99%

An epigenetic switch governing daughter cell separation in Bacillus subtilis

Chai¹,

Norman²,

Kolter³

et al. 2010

Genes Dev.

167

243

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Growing cells of Bacillus subtilis are a bistable mixture of individual motile cells in which genes for daughter cell separation and motility are ON, and chains of sessile cells in which these genes are OFF. How this ON/OFF switch is controlled has been mysterious. Here we report that a complex of the SinR and SlrR proteins binds to and represses genes involved in cell separation and motility. We also report that SinR and SlrR constitute a double-negative feedback loop in which SinR represses the gene for SlrR (slrR), and, by binding to (titrating) SinR, SlrR prevents SinR from repressing slrR. Thus, SlrR indirectly derepresses its own gene, creating a self-reinforcing loop. Finally, we show that, once activated, the loop remains locked in a high SlrR state in which cell separation and motility genes are OFF for extended periods of time. SinR and SlrR constitute an epigenetic switch for controlling genes involved in cell separation and motility.

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“…The XRE family of transcriptional regulators constitute a large family of proteins with a helix-turn-helix DNA-binding motif similar to that of the CI repressor and the Cro proteins of bacteriophage (9 -11), the Bacillus subtilis SinR protein (12), and the restriction modification system control proteins such as C.PvII and C.AhdI (13,14). These proteins make specific DNA contacts through their N-terminal domains, but their DNA binding affinity is modulated by their C-terminal domains (15,16). The members of the helix-turn-helix XRE family are monomers, dimers, or tetramers in solution and bind to the DNA as homodimers or heterodimers (8,17,18).…”

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confidence: 99%

Biochemical Characterization of the Transcriptional Regulator BzdR from Azoarcus sp. CIB

Durante‐Rodríguez

Valderrama

Mancheño

et al. 2010

Journal of Biological Chemistry

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The BzdR transcriptional regulator that controls the P N promoter responsible for the anaerobic catabolism of benzoate in Azoarcus sp. CIB constitutes the prototype of a new subfamily of transcriptional regulators. Here, we provide some insights about the functional-structural relationships of the BzdR protein. Analytical ultracentrifugation studies revealed that BzdR is homodimeric in solution. An electron microscopy three-dimensional reconstruction of the BzdR dimer has been obtained, and the predicted structures of the respective N-and C-terminal domains of each BzdR monomer could be fitted into such a reconstruction. Gel retardation and ultracentrifugation experiments have shown that the binding of BzdR to its cognate promoter is cooperative. Different biochemical approaches revealed that the effector molecule benzoyl-CoA induces conformational changes in BzdR without affecting its oligomeric state. The BzdRdependent inhibition of the P N promoter and its activation in the presence of benzoyl-CoA have been established by in vitro transcription assays. The monomeric BzdR4 and BzdR5 mutant regulators revealed that dimerization of BzdR is essential for DNA binding. Remarkably, a BzdR⌬L protein lacking the linker region connecting the N-and C-terminal domains of BzdR is also dimeric and behaves as a super-repressor of the P N promoter. These data suggest that the linker region of BzdR is not essential for protein dimerization, but rather it is required to transfer the conformational changes induced by the benzoyl-CoA to the DNA binding domain leading to the release of the repressor. A model of action of the BzdR regulator has been proposed.

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An evolutionary link between sporulation and prophage induction in the structure of a repressor:anti-repressor complex

Cited by 98 publications

References 31 publications

Cell Death in Pseudomonas aeruginosa Biofilm Development

Cell Death in Pseudomonas aeruginosa Biofilm Development

An epigenetic switch governing daughter cell separation in Bacillus subtilis

Biochemical Characterization of the Transcriptional Regulator BzdR from Azoarcus sp. CIB

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