bofC Encodes a Putative Forespore Regulator of the Bacillus Subtilis σk Checkpoint

Gomez, Manuel; Cutting, Simon M.

doi:10.1099/00221287-143-1-157

Cited by 24 publications

(26 citation statements)

References 31 publications

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“…The gene encoding a spore catalase required for hydrogen peroxide resistance, katX, is part of the F regulon (12), as is gpr, encoding a protease specific for SASPs (see below) (285). In addition, three other genes with roles during sporulation have been identified as being regulated by F : bofC, an additional regulator of K activity (97), and two regulators of F activity, lonB (4,263) and rsfA (306). Therefore, primary functions of F are to couple prespore-and mother cell-specific gene expression and to direct synthesis of the late prespore transcription factor G .…”

Section: F Regulonmentioning

confidence: 99%

“…The genes important for sporulation include spoIIIG, leading to an autocatalytic loop (142, 282); spoIVB, a serine peptidase that signals from the prespore to the mother cell to activate K (39); the spoVA operon, which is required for dipicolinic acid uptake into the prespore from the mother cell (63,202,289); spoVT, a regulator of G -dependent gene expression (13); and bofC, a regulator of pro-K processing (97,296). The germination genes include the gerA operon, involved with germination in response to alanine; the homologous gerB operon, involved with germination in response to a panel of germinants (L-asparagine, glucose, fructose, and potassium ions) (213); and pdaA, which is required for the formation of muramic ␦-lactam, a unique component of spore cortex peptidoglycan (89).…”

Section: G Regulonmentioning

confidence: 99%

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Compartmentalization of Gene Expression duringBacillus subtilisSpore Formation

Hilbert

Piggot

2004

Microbiol Mol Biol Rev

318

432

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Gene expression in members of the family Bacillaceae becomes compartmentalized after the distinctive, asymmetrically located sporulation division. It involves complete compartmentalization of the activities of sporulation-specific sigma factors, σF in the prespore and then σE in the mother cell, and then later, following engulfment, σG in the prespore and then σK in the mother cell. The coupling of the activation of σF to septation and σG to engulfment is clear; the mechanisms are not. The σ factors provide the bare framework of compartment-specific gene expression. Within each σ regulon are several temporal classes of genes, and for key regulators, timing is critical. There are also complex intercompartmental regulatory signals. The determinants for σF regulation are assembled before septation, but activation follows septation. Reversal of the anti-σF activity of SpoIIAB is critical. Only the origin-proximal 30% of a chromosome is present in the prespore when first formed; it takes ≈15 min for the rest to be transferred. This transient genetic asymmetry is important for prespore-specific σF activation. Activation of σE requires σF activity and occurs by cleavage of a prosequence. It must occur rapidly to prevent the formation of a second septum. σG is formed only in the prespore. SpoIIAB can block σG activity, but SpoIIAB control does not explain why σG is activated only after engulfment. There is mother cell-specific excision of an insertion element in sigK and σE-directed transcription of sigK, which encodes pro-σK. Activation requires removal of the prosequence following a σG-directed signal from the prespore

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Section: F Regulonmentioning

confidence: 99%

Section: G Regulonmentioning

confidence: 99%

Compartmentalization of Gene Expression duringBacillus subtilisSpore Formation

Hilbert

Piggot

2004

Microbiol Mol Biol Rev

318

432

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“…RNA polymerase containing K (E K ) transcribes mother cell genes encoding spore coat proteins, as well as later-acting factors involved in the release of the spore from the mother cell and in spore germination. The K checkpoint ensures that K becomes active in the mother cell only at the appropriate stage of forespore development, which is ϳ3 h after the onset of sporulation (4,5). Premature activation of K , by as little as 30 min, leads to aberrant spore formation (6).…”

mentioning

confidence: 99%

“…1). bofC was discovered as a gene whose deletion in a spoIIIG (which encodes G ) null mutant background restores signaling of pro-K processing, giving rise to a Bof phenotype (4). This suggests that BofC is able to inhibit pro-K processing by SpoIVB but only when the latter is present at the low concentrations produced by E F .…”

mentioning

confidence: 99%

The Structure of Bypass of Forespore C, an Intercompartmental Signaling Factor during Sporulation in Bacillus

Patterson

Brannigan

Cutting

et al. 2005

Journal of Biological Chemistry

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Sporulation in Bacillus subtilis begins with an asymmetric cell division giving rise to smaller forespore and larger mother cell compartments. Different programs of gene expression are subsequently directed by compartment-specific RNA polymerase -factors. In the final stages, spore coat proteins are synthesized in the mother cell under the control of RNA polymerase containing K , (E K ).K is synthesized as an inactive zymogen, pro-K , which is activated by proteolytic cleavage. Processing of pro-K is performed by SpoIVFB, a metalloprotease that resides in a complex with SpoIVFA and bypass of forespore (Bof)A in the outer forespore membrane. Ensuring coordination of events taking place in the two compartments, pro-K processing in the mother cell is delayed until appropriate signals are received from the forespore. Cell-cell signaling is mediated by SpoIVB and BofC, which are expressed in the forespore and secreted to the intercompartmental space where they regulate pro-K processing by mechanisms that are not yet fully understood. Here we present the three-dimensional structure of BofC determined by solution state NMR. BofC is a monomer made up of two domains. The N-terminal domain, containing a four-stranded ␤-sheet onto one face of which an ␣-helix is packed, closely resembles the third immunoglobulin-binding domain of protein G from Streptococcus. The C-terminal domain contains a three-stranded ␤-sheet and three ␣-helices in a novel domain topology. The sequence connecting the domains contains a conserved DISP motif to which mutations that affect BofC activity map. Possible roles for BofC in the K checkpoint are discussed in the light of sequence and structure comparisons.In response to starvation, Bacillus subtilis and its relatives have the remarkable capacity to abandon growth and embark on a developmental pathway that leads to the production of dormant spores that are resistant to a variety of physical stresses. Sporulation begins with an asymmetric septation, which gives rise to two cells of unequal size but with identical chromosomes. The smaller cell is called the forespore, as it is destined to mature into the resistant spore, whereas the larger compartment is referred to as the mother cell, because it subsequently engulfs the forespore and nurtures the latter during its development. In the final stages, the mother cell lyses, and the mature spore is released into the environment where it can remain dormant indefinitely, germinating when favorable conditions for growth are restored (1).A hallmark of sporulation is the utilization of a series of spatially and temporally regulated RNA polymerase -factors to effect differential gene expression from the identical chromosomes present in the forespore and the mother cell.

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“…tein interaction (11,38). Premature signaling is also prevented by two inhibitors, SpoIVFA and BofA, which are thought to maintain the SpoIVFB protease in an inactive state (5,25,27).…”

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confidence: 99%

The PDZ Domain of the SpoIVB Serine Peptidase Facilitates Multiple Functions

2001

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During spore formation in Bacillus subtilis, the SpoIVB protein is a critical component of the K regulatory checkpoint. SpoIVB has been shown to be a serine peptidase that is synthesized in the spore chamber and which self-cleaves, releasing active forms. These forms can signal proteolytic processing of the transcription factor K in the outer mother cell chamber of the sporulating cell. This forms the basis of the K checkpoint and ensures accurate K -controlled gene expression. SpoIVB has also been shown to activate a second distinct process, termed the second function, which is essential for the formation of heat-resistant spores. In addition to the serine peptidase domain, SpoIVB contains a PDZ domain. We have altered a number of conserved residues in the PDZ domain by site-directed mutagenesis and assayed the sporulation phenotype and signaling properties of mutant SpoIVB proteins. Our work has revealed that the SpoIVB PDZ domain could be used for up to four distinct processes, (i) targeting of itself for trans proteolysis, (ii) binding to the protease inhibitor BofC, (iii) signaling of pro-K processing, and (iv) signaling of the second function of SpoIVB.

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bofC Encodes a Putative Forespore Regulator of the Bacillus Subtilis σk Checkpoint

Cited by 24 publications

References 31 publications

Compartmentalization of Gene Expression duringBacillus subtilisSpore Formation

Compartmentalization of Gene Expression duringBacillus subtilisSpore Formation

The Structure of Bypass of Forespore C, an Intercompartmental Signaling Factor during Sporulation in Bacillus

The PDZ Domain of the SpoIVB Serine Peptidase Facilitates Multiple Functions

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