A novel regulatory protein governing biofilm formation in <i>Bacillus subtilis</i>

Chu, Frances; Kearns, Daniel B.; McLoon, Anna L.; Chai, Yunrong; Kolter, Roberto; Losick, Richard

doi:10.1111/j.1365-2958.2008.06201.x

Cited by 139 publications

(191 citation statements)

References 25 publications

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“…AbrB is a key transition-state regulator in Bacillus subtilis that affects the regulation of postexponential gene expression (Strauch and Hoch 1993;Phillips and Strauch 2002) and biofilm-forming gene expression (Chu et al 2008). cyAbrBs show rather low similarity to AbrB in amino acid sequence, but possess a bbabb structure at the C-terminal region that is characteristic of AbrB-like DNA-binding domains (Ishii and Hihara 2008).…”

Section: Introductionmentioning

confidence: 99%

CalA, a cyAbrB protein, binds to the upstream region of ftsZ and is down-regulated in heterocysts in Anabaena sp. PCC 7120

2010

Arch Microbiol

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A protein of cyAbrB family of regulators, Alr0946 (CalA), was identified by DNA affinity chromatography using DNA fragments from the promoter region of ftsZ in Anabaena/Nostoc sp. PCC 7120. Electrophoretic mobility shift assays showed that the protein could bind to upstream regions of ftsZ (as biotin-labeled DNA fragments) and that the binding was inhibited by the same DNA fragments and a fragment upstream of hetC but not by 3 fragments upstream of glnA, hetR or ntcA. Both transcriptional fusion with gfp (green fluorescence protein) and Western blot analysis indicated that the expression of calA was down-regulated in heterocysts relative to vegetative cells. An insertional mutant of calA could not be completely segregated. Over-expression of calA in Anabaena/ Nostoc caused no change in growth, heterocyst differentiation or expression of ftsZ. CalA as a DNA-binding protein is essential for the growth of Anabaena/Nostoc and may be required for the expression of ftsZ in vegetative cells.

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Section: Introductionmentioning

confidence: 99%

CalA, a cyAbrB protein, binds to the upstream region of ftsZ and is down-regulated in heterocysts in Anabaena sp. PCC 7120

2010

Arch Microbiol

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“…Biofilm formation is governed by a regulatory circuit that involves three dedicated regulatory proteins: SinI, SinR, and SlrR Chu et al 2008;Kobayashi 2008). SinI is produced under the control of Spo0A, a global regulator of post-exponential-phase gene expression in B. subtilis (Gaur et al 1988;Sonenshein 2000;Piggot and Hilbert 2004;Fujita et al 2005;Chai et al 2008).…”

mentioning

confidence: 99%

“…SinR, in turn, binds to the promoters for matrix operons (yqxM and eps [exopolysaccharide]) and the gene for SlrR (slrR), blocking their transcription ( Fig. 1A; Branda et al 2006;Chu et al 2006Chu et al , 2008. SlrR is a hybrid protein, containing domains that are homologous to both the SinI anti-repressor and the SinR repressor .…”

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confidence: 99%

An epigenetic switch governing daughter cell separation in Bacillus subtilis

Chai¹,

Norman²,

Kolter³

et al. 2010

Genes Dev.

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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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“…A survey of genes required for efficient biofilm formation in B. subtilis revealed that a med mutation confers a modest defect in biofilm colony morphology (9). Biofilms are composed of long chains of cells that are held together by an extracellular matrix consisting of protein and polysaccharide.…”

Section: Resultsmentioning

confidence: 99%

Phosphorylation of Spo0A by the Histidine Kinase KinD Requires the Lipoprotein Med in Bacillus subtilis

2011

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The response regulatory protein Spo0A of Bacillus subtilis is activated by phosphorylation by multiple histidine kinases via a multicomponent phosphorelay. Here we present evidence that the activity of one of the kinases, KinD, depends on the lipoprotein Med, a mutant of which has been known to cause a cannibalism phenotype. We show that the absence of Med impaired and the overproduction of Med stimulated the transcription of two operons (sdp and skf) involved in cannibalism whose transcription is known to depend on Spo0A in its phosphorylated state (Spo0AϳP). Further, these effects of Med were dependent on KinD but not on kinases KinA, KinB, and KinC. Additionally, we show that deletion or overproduction of Med impaired or enhanced, respectively, biofilm formation and that these effects, too, depended specifically on KinD. Finally, we report that overproduction of Med bypassed the dominant negative effect on transcription of sdp of a truncated KinD retaining the transmembrane segments but lacking the kinase domain. We propose that Med directly or indirectly interacts with KinD in the cytoplasmic membrane and that this interaction is required for KinDdependent phosphorylation of Spo0A.

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A novel regulatory protein governing biofilm formation in Bacillus subtilis

Cited by 139 publications

References 25 publications

CalA, a cyAbrB protein, binds to the upstream region of ftsZ and is down-regulated in heterocysts in Anabaena sp. PCC 7120

CalA, a cyAbrB protein, binds to the upstream region of ftsZ and is down-regulated in heterocysts in Anabaena sp. PCC 7120

An epigenetic switch governing daughter cell separation in Bacillus subtilis

Phosphorylation of Spo0A by the Histidine Kinase KinD Requires the Lipoprotein Med in Bacillus subtilis

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