Cyclic diguanylate regulation of <i>Bacillus cereus</i> group biofilm formation

Fagerlund, Annette; Smith, Veronika; Røhr, Åsmund K.; Lindbäck, Toril; Parmer, Marthe Petrine; Andersson, K. Kristoffer; Reubsaet, Léon; Økstad, Ole Andreas

doi:10.1111/mmi.13405

Cited by 40 publications

(73 citation statements)

References 105 publications

(141 reference statements)

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“…However, members of the B . cereus group contain the ortholog gene cdgA (Fagerlund et al, 2016) but no operon similar to ydaJ - M of B. subtilis . Considering this, our study cannot exclude the possibility that DgcK affects other c-di-GMP signaling pathways even in B. subtilis via different effector proteins.…”

Section: Discussionmentioning

confidence: 99%

New Functions and Subcellular Localization Patterns of c-di-GMP Components (GGDEF Domain Proteins) in B. subtilis

Bedrunka

Graumann

2017

Front. Microbiol.

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The universal and pleiotropic cyclic dinucleotide second messenger c-di-GMP is most prominently known to inversely regulate planktonic and sessile lifestyles of Gram-negative species. In the Gram-positive model organism Bacillus subtilis, intracellular c-di-GMP levels are modulated by a concise set of three diguanylate cylases (DgcK, DgcP, DgcW) and one phosphodiesterase (PdeH). Two recent studies have reported the negative influence of the c-di-GMP receptor DgrA (PilZ domain protein) on swarming motility indicating a conserved role of this second messenger across the bacterial domain. However, it has been suggested that the degenerated GGDEF protein YdaK and the inactive EAL domain protein YkuI may also function as c-di-GMP receptors regulating potentially other processes than motility. Here we describe a novel c-di-GMP dependent signaling network in B. subtilis regulating the production of an unknown exopolysaccharide (EPS) that leads to strongly altered colony morphologies upon overproduction. The network consists of the c-di-GMP receptor YdaK and the c-di-GMP synthetase DgcK. Both proteins establish a spatially close signal-effector cluster at the membrane. The cytoplasmic DgcP synthetase can complement for DgcK only upon overproduction, while the third c-di-GMP synthetase, DgcW, of B. subtilis is not part of the signaling pathway. Removal of the regulatory EAL domain from DgcW reveals a distinct function in biofilm formation. Therefore, our study is compatible with the “local pool signaling” hypothesis, but shows that in case of the yda operon, this can easily be overcome by overproduction of non-cognate DGCs, indicating that global pools can also confer signals to regulatory circuits in a Gram-positive bacterium.

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Section: Discussionmentioning

confidence: 99%

New Functions and Subcellular Localization Patterns of c-di-GMP Components (GGDEF Domain Proteins) in B. subtilis

Bedrunka

Graumann

2017

Front. Microbiol.

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“…cereus [10]. The fla-che operon contains genes encoding components of the flagella and chemotaxis machinery, as well as the alternative sigma factor, σ D [11].…”

Section: Resultsmentioning

confidence: 99%

Intracellular Zn(II) Intoxication Leads to Dysregulation of the PerR Regulon Resulting in Heme Toxicity in Bacillus subtilis

Chandrangsu

Helmann

2016

PLoS Genet

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Transition metal ions (Zn(II), Cu(II)/(I), Fe(III)/(II), Mn(II)) are essential for life and participate in a wide range of biological functions. Cellular Zn(II) levels must be high enough to ensure that it can perform its essential roles. Yet, since Zn(II) binds to ligands with high avidity, excess Zn(II) can lead to protein mismetallation. The major targets of mismetallation, and the underlying causes of Zn(II) intoxication, are not well understood. Here, we use a forward genetic selection to identify targets of Zn(II) toxicity. In wild-type cells, in which Zn(II) efflux prevents intoxication of the cytoplasm, extracellular Zn(II) inhibits the electron transport chain due to the inactivation of the major aerobic cytochrome oxidase. This toxicity can be ameliorated by depression of an alternate oxidase or by mutations that restrict access of Zn(II) to the cell surface. Conversely, efflux deficient cells are sensitive to low levels of Zn(II) that do not inhibit the respiratory chain. Under these conditions, intracellular Zn(II) accumulates and leads to heme toxicity. Heme accumulation results from dysregulation of the regulon controlled by PerR, a metal-dependent repressor of peroxide stress genes. When metallated with Fe(II) or Mn(II), PerR represses both heme biosynthesis (hemAXCDBL operon) and the abundant heme protein catalase (katA). Metallation of PerR with Zn(II) disrupts this coordination, resulting in depression of heme biosynthesis but continued repression of catalase. Our results support a model in which excess heme partitions to the membrane and undergoes redox cycling catalyzed by reduced menaquinone thereby resulting in oxidative stress.

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“…Strikingly, biofilm formation is not affected by the deletion of all diguanylate cyclases in B. subtilis suggesting different mechanisms of signal transduction in this bacterium. In contrast, the major diguanylate cyclase CdgF is essential for biofilm formation in Bacillus thurigiensis (Fagerlund et al ., ). Consistent with the c‐di‐GMP independent biofilm formation in B. subtilis , this enzyme does not have a counterpart in B. subtilis .…”

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confidence: 97%

Cyclic‐di‐GMP signalling meets extracellular polysaccharide synthesis in Bacillus subtilis

Kampf

Stülke

2017

Environ Microbiol Rep

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In order to resist harmful environmental conditions, many bacteria form multicellular aggregates called biofilms. In these biofilms, they protect themselves in a self-produced matrix consisting of extracellular polysaccharides, proteins and DNA. In many bacteria, biofilm formation is stimulated in the presence of the second messenger cyclic di-GMP. In this issue of Environmental Microbiology Reports, Bedrunka and Graumann have studied matrix production by the proteins encoded in the Bacillus subtilis ydaJKLMN operon. For the first time, they were able to provide a link between c-di-GMP signalling and matrix production in this bacterium. The work demonstrates that the c-di-GMP receptor protein YdaK forms a membrane-bound complex with the YdaM and YdaN proteins, and that this interaction with YdaK is required for polysaccharide production by YdaL, YdaM and YdaN.

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Cyclic diguanylate regulation of Bacillus cereus group biofilm formation

Cited by 40 publications

References 105 publications

New Functions and Subcellular Localization Patterns of c-di-GMP Components (GGDEF Domain Proteins) in B. subtilis

New Functions and Subcellular Localization Patterns of c-di-GMP Components (GGDEF Domain Proteins) in B. subtilis

Intracellular Zn(II) Intoxication Leads to Dysregulation of the PerR Regulon Resulting in Heme Toxicity in Bacillus subtilis

Cyclic‐di‐GMP signalling meets extracellular polysaccharide synthesis in Bacillus subtilis

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