Integration of multiple developmental signals in Bacillus subtilis through the Spo0A transcription factor.

Ireton, Keith; Rudner, David Z.; Siranosian, Kathryn Jaacks; Grossman, Alan D.

doi:10.1101/gad.7.2.283

Cited by 247 publications

(225 citation statements)

References 68 publications

(89 reference statements)

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“…Deletions in the amino-terminal region of the protein cause it to become constitutively active even in the absence of phosphorylation (Ireton et al 1993). Expression of one such mutant, sad67, from an IPTG-inducible Pspac promoter during vegetative growth, was sufficient to switch the site of FtsZ assembly from a medial to a polar pattern (Fig.…”

Section: A Constitutively Active Form Of Spooa Is Able To Induce Formmentioning

confidence: 99%

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Transcription factor Spo0A switches the localization of the cell division protein FtsZ from a medial to a bipolar pattern in Bacillus subtilis.

Levin¹,

Losick²

1996

Genes Dev.

247

262

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Entry into sporulation by the Gram-positive bacterium Bacillus subtilis is governed by two transcription factors, SpoOA and cr H, and involves a switch in the site of division from a medial to a polar location. We report that at the onset of sporulation, assembly of the cell division protein FtsZ shifts from midcell to potential division sites near both poles. The switch to a bipolar pattern of FtsZ localization is dependent on Spo0A. Additionally, synthesis of an activated form of Spo0A during growth artificially activates the switch in FtsZ localization and results in the formation of polar septa. The o a factor, on the other hand, is dispensable for the switch in the position of the FtsZ assembly site, although it is required for formation of the polar septum. Our results suggest that during the transition from growth to sporulation, Spo0A induces the expression of genes that suppress FtsZ assembly at the midcell site and activate sites at both poles, whereas O "H induces genes required for a subsequent step in cytokinesis.

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Section: A Constitutively Active Form Of Spooa Is Able To Induce Formmentioning

confidence: 99%

“…2, part I, P-R). Moreover, the production of an activated form of SpoOA (Sad67) (Ireton et al 1993) in growing cells switched the assembly site of FtsZ from medial to polar positions (Fig. 2, part I, S-U) and induced the formation of polar septa (Fig.…”

Section: Genes and Development 483mentioning

confidence: 99%

Transcription factor Spo0A switches the localization of the cell division protein FtsZ from a medial to a bipolar pattern in Bacillus subtilis.

Levin¹,

Losick²

1996

Genes Dev.

247

262

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“…The Muta-Gene M13 in vitro mutagenesis kit (BioRad) was used to obtain the crh1 (crhS46A) allele. A 434-bp PvuII-BstBI DNA fragment containing the promoterless crh gene or crh1 allele was inserted in pDR67 (26) cut with SmaI and ClaI to give plasmid pRC16 or pRC17, respectively. Plasmid pDR67 carries the pC194 chloramphenicol acetyltransferase gene cat and a spac promoter between two fragments of the B. subtilis amyE gene.…”

Section: Methodsmentioning

confidence: 99%

The Bacillus subtilis crh gene encodes a HPr-like protein involved in carbon catabolite repression

Galinier

Haiech

Kilhoffer

et al. 1997

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

208

274

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Carbon catabolite repression (CCR) of several Bacillus subtilis catabolic genes is mediated by ATPdependent phosphorylation of histidine-containing protein (HPr), a phosphocarrier protein of the phosphoenolpyruvate (PEP): sugar phosphotransferase system. In this study, we report the discovery of a new B. subtilis gene encoding a HPr-like protein, Crh (for catabolite repression HPr), composed of 85 amino acids. Crh exhibits 45% sequence identity with HPr, but the active site His-15 of HPr is replaced with a glutamine in Crh. Crh is therefore not phosphorylated by PEP and enzyme I, but is phosphorylated by ATP and the HPr kinase in the presence of fructose-1,6-bisphosphate. We determined Ser-46 as the site of phosphorylation in Crh by carrying out mass spectrometry with peptides obtained by tryptic digestion or CNBr cleavage. In a B. subtilis ptsH1 mutant strain, synthesis of ␤-xylosidase, inositol dehydrogenase, and levanase was only partially relieved from CCR. Additional disruption of the crh gene caused almost complete relief from CCR. In a ptsH1 crh1 mutant, producing HPr and Crh in which Ser-46 is replaced with a nonphosphorylatable alanyl residue, expression of ␤-xylosidase was also completely relieved from glucose repression. These results suggest that CCR of certain catabolic operons requires, in addition to CcpA, ATP-dependent phosphorylation of Crh, and HPr at Ser-46.The bacterial phosphoenolpyruvate (PEP): sugar phosphotransferase system (PTS) catalyzes the transport and concomitant phosphorylation of carbohydrates via a protein phosphorylation chain including PEP-dependent phosphorylation of His-15 in histidine-containing protein (HPr) by enzyme I (EI). P-His-HPr phosphorylates the sugar-specific EIIAs. In Gram-positive bacteria, the PTS regulates also induction and carbon catabolite repression (CCR) of numerous catabolic genes (1). The central regulatory protein involved in these various functions is HPr. In Gram-positive bacteria, this small phosphoryl transfer protein can be phosphorylated at a regulatory serine (Ser-46) by ATP and the HPr kinase (2, 3), in addition to phosphorylation at the catalytic His-15 by PEP and EI (4, 5). PEP-dependent and ATP-dependent phosphorylation of HPr interfere with each other-i.e., P-His-HPr is a poor substrate for the HPr kinase and P-Ser-HPr is a poor substrate for EI (6, 7). ATP-dependent phosphorylation of HPr is stimulated by glycolytic intermediates such as fructose-1,6-bisphosphate (FBP) in Enterococcus faecalis (6) and in Streptococcus pyogenes (7). It has been reported that FBP is also implicated in CCR of the Bacillus subtilis gnt and iol operons (8, 9), and a potential role of phosphorylation of HPr at Ser-46 in CCR has therefore been investigated (10). The gnt operon contains the genes gntRKPZ encoding the repressor GntR, gluconate kinase, gluconate permease, and a gluconate-6-Pdehydrogenase (11), whereas the iol operon is composed of 10 genes encoding enzymes presumably implicated in inositol metabolism, including iolG encoding inositol dehydro...

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“…If Soj regulates sporulation by decreasing Spo0A phosphorylation, then a mutant form of Spo0A (called Spo0A Sad67 ) (15) that can activate gene expression and sporulation in an unphosphorylated state ought to bypass the sporulation defect of a ⌬spo0J mutant. Expression of spo0A sad67 from the Pspac promoter permits wild-type sporulation levels in cells that cannot phosphorylate Spo0A and allows Spo0AϳP-activated gene We compared sporulation in ⌬spo0J cells carrying either Pspac-spo0A ϩ or Pspac-spo0A sad67 .…”

Section: Resultsmentioning

confidence: 99%

“…The ⌬spo0J::spc and ⌬(soj-spo0J)::spc deletion-insertions were previously described (14). The Pspacspo0A ϩ and Pspac-spo0A sad67 constructs were previously described (15). The spoIIG-lacZ fusion (17) is located in the specialized transducing phage SP␤.…”

Section: Methodsmentioning

confidence: 99%

Control of Sporulation Gene Expression in Bacillus subtilis by the Chromosome Partitioning Proteins Soj (ParA) and Spo0J (ParB)

Quisel

Grossman

2000

J Bacteriol

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Two chromosome partitioning proteins, Soj (ParA) and Spo0J (ParB), regulate the initiation of sporulation in Bacillus subtilis. In a spo0J null mutant, sporulation is inhibited by the action of Soj. Soj negatively regulates expression of several sporulation genes by binding to the promoter regions and inhibiting transcription. All of the genes known to be inhibited by Soj are also activated by the phosphorylated form of the transcription factor Spo0A (Spo0AϳP). We found that, in a spo0J null mutant, Soj affected sporulation, in part, by decreasing the level of Spo0A protein. Soj negatively regulated transcription of spo0A and associated with the spo0A promoter region in vivo. Expression of spo0A from a heterologous promoter in a spo0J null mutant restored Spo0A levels and partly bypassed the sporulation and gene expression defects. Soj did not appear to significantly affect phosphorylation of Spo0A. Thus, in the absence of Spo0J, Soj inhibits sporulation and sporulation gene expression by inhibiting accumulation of the activator protein Spo0A and by acting downstream of Spo0A to inhibit gene expression directly.Bacillus subtilis can sporulate in response to starvation and high cell density. Sporulation involves an asymmetric cell division and requires DNA replication and chromosome segregation. Spo0A is a critical transcription factor in early sporulation. Cells initiate sporulation when they accumulate a threshold amount of phosphorylated Spo0A (Spo0AϳP) (3,6,12). Many signals that regulate sporulation do so by affecting the accumulation of Spo0AϳP. Spo0A obtains phosphate from a set of proteins called the phosphorelay (2). A balance of kinases and phosphatases regulates phosphate input into the phosphorelay and the phosphorylation state of Spo0A (3,(30)(31)(32).Two proteins involved in chromosome partitioning, Soj and Spo0J, also regulate the initiation of sporulation, perhaps in response to chromosome structure or partitioning (4,14,28). Soj and Spo0J are members of the ParA-SopA and ParB-SopB protein families, respectively. Many ParA-and ParB-type proteins are encoded on low-copy-number plasmids and are required for accurate plasmid partitioning (29, 42). Chromosome-encoded family members have also been identified, several of which function in chromosome partitioning (14,22,26). Members of the ParA-SopA families can act as transcriptional repressors and are themselves often regulated by members of the ParB-SopB family (7,9,24,27,36).Spo0J is required both for accurate chromosome partitioning and for sporulation (14). Spo0J binds to a series of sites (parS sites) in the origin-proximal 20% of the chromosome (22), clustering them into a large focus (10,21,23). Defects in spo0J perturb chromosome partitioning. Cultures of spo0J null mutant cells produce approximately 1% anucleate cells, a frequency approximately 20-to 100-fold greater than that of wildtype cells (14).A null mutation in spo0J also causes an approximately 300-fold defect in sporulation relative to wild-type cells (14,28,34). spo0J null mutants ar...

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Integration of multiple developmental signals in Bacillus subtilis through the Spo0A transcription factor.

Cited by 247 publications

References 68 publications

Transcription factor Spo0A switches the localization of the cell division protein FtsZ from a medial to a bipolar pattern in Bacillus subtilis.

Transcription factor Spo0A switches the localization of the cell division protein FtsZ from a medial to a bipolar pattern in Bacillus subtilis.

The Bacillus subtilis crh gene encodes a HPr-like protein involved in carbon catabolite repression

Control of Sporulation Gene Expression in Bacillus subtilis by the Chromosome Partitioning Proteins Soj (ParA) and Spo0J (ParB)

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