Compartmentalized distribution of the proteins controlling the prespore‐specific transcription factor σF of Bacillus subtilis

Lewis, Peter J.; Magnin, Thierry; Errington, Jeff

doi:10.1046/j.1365-2443.1996.750275.x

Cited by 42 publications

(58 citation statements)

References 46 publications

(101 reference statements)

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“…These results are seemingly at odds with the contention that unphosphorylated SpoIIAA is concentrated in the forespore and that this is the basis for the cell-specific activation of F (Lewis et al 1996). As presented above, only ∼8% of the cells had formed polar septa by 90 min.…”

Section: Appearance Of Unphosphorylated Spoiiaa During the Onset Of Smentioning

confidence: 81%

“…Cold Spring Harbor Laboratory Press on May 8, 2018 -Published by genesdev.cshlp.org Downloaded from (SpoIIAA and SpoIIAA-P) is evenly distributed throughout the sporangium (Lewis et al 1996), and because the volume of the forespore is much smaller than that of the mother cell, if SpoIIAA-P were dephosphorylated exclusively in the forespore, only a small proportion (<20%) of the total SpoIIAA in the sporangium should be unphosphorylated. Therefore, the results of the time-course experiments are most easily compatible with the view that unphosphorylated SpoIIAA is present in the predivisional sporangium and the mother cell as well as in the forespore.…”

Section: Regulation Of F Genes and Development 1161mentioning

confidence: 99%

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Septation, dephosphorylation, and the activation of sigma F during sporulation in Bacillus subtilis

King

Dreesen²,

Stragier³

et al. 1999

Genes & Development

124

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Cell-specific activation of transcription factor F during sporulation in Bacillus subtilis requires the formation of the polar septum and the activity of a serine phosphatase (SpoIIE) located in the septum. The SpoIIE phosphatase indirectly activates F by dephosphorylating a protein (SpoIIAA-P) in the pathway that controls the activity of the transcription factor. By use of a SpoIIE-GFP fusion protein in time-course and time-lapse experiments and by direct visualization of septa in living cells, we show that SpoIIE is present in the predivisional sporangium, where it often localizes near both cell poles in structures known as E-rings. We also present evidence consistent with the view that SpoIIE is present in both progeny cells after polar division. These findings are incompatible with a model for the control of F activity in which the phosphatase is simply sequestered to one cell. Instead, we conclude that the function of SpoIIE is subject to regulation, and we present evidence that this occurs in two stages. The first stage, which involves the phosphatase function of SpoIIE, depends on the cell division protein FtsZ and could correspond to the FtsZ-dependent assembly of SpoIIE into E-rings. The second stage occurs after the dephosphorylation of SpoIIAA-P and is dependent on the later-acting, cell-division protein DivIC. Evidence based on the use of modified and mutant forms of the phosphatase protein indicates that SpoIIE blocks the capacity of unphosphorylated SpoIIAA to activate F until formation of the polar septum is completed.

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Section: Appearance Of Unphosphorylated Spoiiaa During the Onset Of Smentioning

confidence: 81%

Section: Regulation Of F Genes and Development 1161mentioning

confidence: 99%

Septation, dephosphorylation, and the activation of sigma F during sporulation in Bacillus subtilis

King

Dreesen²,

Stragier³

et al. 1999

Genes & Development

124

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“…It was shown 25 years ago through a study of genetic mosaics that gene expression is compartmentalized during sporulation of B. subtilis, with different genes being expressed in the prespore and the mother cell, the two cell types involved (43,226). In the years since, the completeness of compartmentalization has been demonstrated first by immunoelectron microscopy (48,83,189), then by fluorescence microscopy with immunofluorescence and green fluorescent protein (105,170,233,299,314), and most recently through the use of a two-part transcriptional probe (173).…”

Section: Introductionmentioning

confidence: 99%

Compartmentalization of Gene Expression duringBacillus subtilisSpore Formation

Hilbert

Piggot

2004

Microbiol Mol Biol Rev

320

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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“…First, in the prespore the SpoIIAB kinase and SpoIIE phosphatase are active simultaneously, and SpoIIAA is continually cycled between the nonphosphorylated and the phosphorylated forms (17). Second, the activity of SpoIIE is much higher than that of SpoIIAB (15), and hence in the prespore all (or almost all) of the SpoIIAA is in the nonphosphorylated form (9,11,13). Third, the intracellular concentrations of SpoIIAB and F are equal, so that there is only just enough SpoIIAB to inhibit F ; thus, the sequestration of even a fraction of the SpoIIAB in an alternative reaction will liberate some F activity (17).…”

mentioning

confidence: 99%

Fate of the SpoIIAB-ADP Liberated after SpoIIAB Phosphorylates SpoIIAA of Bacillus subtilis*

2000

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Phosphorylation of SpoIIAA catalyzed by SpoIIAB helps to regulate the first sporulation-specific factor, F , of Bacillus subtilis. The steady-state rate of phosphorylation is known to be exceptionally slow and to be limited by the return of the protein kinase, SpoIIAB, to a catalytically active state. Previous work from this laboratory has suggested that, after catalyzing the phosphorylation, SpoIIAB is in a form (SpoIIAB*) that does not readily release ADP. We now show that the rate of release of ADP from the SpoIIAB*-ADP complex was much diminished by the presence of unreacted SpoIIAA, suggesting that SpoIIAA can form a long-lived ternary complex with SpoIIAB*-ADP in which the SpoIIAB* form is stabilized. In kinetic studies of the phosphorylation of SpoIIAA, the ternary complex SpoIIAA-SpoIIAB*-ADP could be distinguished from the short-lived complex SpoIIAA-SpoIIAB-ADP, which can be readily produced in the absence of an enzymatic reaction.

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Compartmentalized distribution of the proteins controlling the prespore‐specific transcription factor σ^F of Bacillus subtilis

Cited by 42 publications

References 46 publications

Septation, dephosphorylation, and the activation of sigma F during sporulation in Bacillus subtilis

Septation, dephosphorylation, and the activation of sigma F during sporulation in Bacillus subtilis

Compartmentalization of Gene Expression duringBacillus subtilisSpore Formation

Fate of the SpoIIAB-ADP Liberated after SpoIIAB Phosphorylates SpoIIAA of Bacillus subtilis*

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Compartmentalized distribution of the proteins controlling the prespore‐specific transcription factor σF of Bacillus subtilis

Cited by 42 publications

References 46 publications

Septation, dephosphorylation, and the activation of sigma F during sporulation in Bacillus subtilis

Septation, dephosphorylation, and the activation of sigma F during sporulation in Bacillus subtilis

Compartmentalization of Gene Expression duringBacillus subtilisSpore Formation

Fate of the SpoIIAB*-ADP Liberated after SpoIIAB Phosphorylates SpoIIAA of Bacillus subtilis

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Product

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Compartmentalized distribution of the proteins controlling the prespore‐specific transcription factor σ^F of Bacillus subtilis

Fate of the SpoIIAB-ADP Liberated after SpoIIAB Phosphorylates SpoIIAA of Bacillus subtilis*