<b>Subcellular localization of proteins governing the proteolytic activation of a developmental transcription factor in <i>Bacillus subtilis</i></b>

Resnekov, Orna; Alper, Scott; Losick, Richard

doi:10.1046/j.1365-2443.1996.d01-262.x

Cited by 87 publications

(122 citation statements)

References 49 publications

(64 reference statements)

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“…Mutations in conserved residues in these motifs in SpoIVFB abolished pro-K processing, suggesting that pro-K processing occurs within the membrane (247,311). Consistent with this conclusion, biochemical and cytological experiments have indicated that pro-K , SpoIVFB, SpoIVFA, and BofA all localize to the cell membrane (100,240,249,294,312). Models of how BofA and SpoIVFA effect the negative regulation of SpoIVFB action have undergone a series of changes, perhaps reflecting the complexity of the process (41,100,153,242,249).…”

mentioning

confidence: 59%

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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confidence: 59%

Compartmentalization of Gene Expression duringBacillus subtilisSpore Formation

Hilbert

Piggot

2004

Microbiol Mol Biol Rev

318

432

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“…The anti-SpoIIAA antisera contained antibodies specific for both SpoIIAA and SpoIIAA-P (Diederich et al 1994). Antibodies used in immunofluorescence studies were purified from either crude polyclonal antisera or Protein A purified antibody preparations using a method kindly provided ahead of publication by O. Resnekov (Resnekov et al 1996), as detailed below. Purified proteins were dialysed against phosphate buffered saline (PBS) overnight at 4 ЊC before cross-linking to washed Affi-Gel 10 resin (BioRad).…”

Section: Affinity Purification Of Antibodies and Commercial Antibody mentioning

confidence: 99%

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

1996

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Background: Differential gene expression during sporulation in the prespore and mother cell of Bacillus subtilis is dependent on the correct timing and localization of the activity of specific transcription (j) factors. The first j factor activated is j F , which directs gene expression specifically in the prespore compartment. Release of j F activity is tightly controlled through a series of complex interactions involving an anti-j factor, SpoIIAB, an anti-anti-j factor SpoIIAA and a phosphoprotein phosphatase SpoIIE. In vitro studies have shown that SpoIIAB binds to j F , preventing transcription of the j F regulon, and that it can also phosphorylate SpoIIAA, thereby inactivating it. However, nonphosphorylated SpoIIAA can displace j F from SpoIIAB. The SpoIIE phosphatase provides a means of reactivating SpoIIAA-P.

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“…K is synthesized as an inactive precursor, pro-K , that associates with membranes in cells (13)(14)(15). SpoIVFB is believed to be an I-Clip that processes pro-K to K on the basis of the following: a B. subtilis spoIVFB mutant is defective in processing (14), coexpression of spoIVFB and sigK (encoding pro-K ) in growing B. subtilis allows processing (16,17), SpoIVFB is a membrane protein (18) with sequence similarity to the S2P family of I-Clips (4,5,19), and mutational analysis of conserved motifs in apparent transmembrane segments of SpoIVFB supports the idea that it is a metalloprotease (4,5). However, as is the case for all I-Clips, cleavage of a physiological substrate in vitro with purified enzyme has not been accomplished.…”

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confidence: 99%

“…SpoIVFB forms a complex with SpoIVFA and BofA in the outer forespore membrane (OFM) (Fig. 1) (18,20). This (21).…”

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confidence: 99%

BofA protein inhibits intramembrane proteolysis of pro-σ^Kin an intercompartmental signaling pathway duringBacillus subtilissporulation

Zhou

Kroos

2004

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

119

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Bacillus subtilis is a bacterium that undergoes a developmental program of sporulation in response to starvation. At the core of the program are factors, whose regulated spatiotemporal activation controls much of the gene expression. Activation of pro-K in the mother cell compartment involves regulated intramembrane proteolysis (RIP) in response to a signal from the forespore. RIP is a poorly understood process that is conserved in prokaryotes and eukaryotes. Here, we report a powerful system for studying RIP of pro-K . Escherichia coli was engineered to coexpress the putative membrane-embedded metalloprotease SpoIVFB with pro-K and potential inhibitors of RIP. Overproduction of SpoIVFB and pro-K in E. coli allowed accurate and abundant proteolytic processing of pro-K with the characteristics expected for SpoIVFB acting as an intramembrane-cleaving protease (I-Clip). Coexpression of BofA in this system led to formation of a BofA-SpoIVFB complex and marked inhibition of pro-K processing. Mutational analysis identified amino acids in BofA that are necessary for complex formation and inhibition of processing, leading us to propose that BofA inhibits SpoIVFB metalloprotease activity by providing a metal ligand, analogous to the cysteine switch mechanism of matrix metalloprotease regulation. The approach described herein should be applicable to studies of other RIP events and amenable to developing in vitro assays for I-Clips.T he abilities of cells to send signals, and to sense and respond to signals from other cells or from the environment, are essential features of developmental and adaptive processes. Regulated intramembrane proteolysis (RIP) has emerged as an important and widely conserved mechanism for controlling signaling pathways in both prokaryotes and eukaryotes (1). RIP involves cleavage of a protein in a transmembrane domain, releasing a part of the protein that in most cases regulates transcription or acts as a signal. Proteases believed to catalyze intramembrane cleavage occur in large families that are typically conserved from archaea to humans, and sometimes in bacteria as well (2). For example, one of the first intramembrane-cleaving proteases (I-Clips) identified, human site-2 protease (S2P) (3), has orthologs in Bacillus subtilis (SpoIVFB) (4, 5) and Escherichia coli (YaeL) (6, 7). Also, Drosophila and bacterial I-Clips in the rhomboid family recognize the same substrate motif and can be functionally interchanged (8, 9). RIP has been implicated in generating bacterial mating (10) and quorum sensing signals (11), and in the extracytoplasmic stress response of E. coli (6, 7). In metazoans, RIP is believed to control the unfolded protein stress response, cholesterol and fatty acid biosynthesis, epidermal growth factor and ErbB4 receptor signaling, Notch signaling, and processing of the Alzheimer precursor protein (1, 2). Elucidating mechanisms of RIP is important for understanding diverse signaling pathways and potentially for treating disease.Bacterial sporulation provides a model to study RIP. When...

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Subcellular localization of proteins governing the proteolytic activation of a developmental transcription factor in Bacillus subtilis

Cited by 87 publications

References 49 publications

Compartmentalization of Gene Expression duringBacillus subtilisSpore Formation

Compartmentalization of Gene Expression duringBacillus subtilisSpore Formation

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

BofA protein inhibits intramembrane proteolysis of pro-σ^Kin an intercompartmental signaling pathway duringBacillus subtilissporulation

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Subcellular localization of proteins governing the proteolytic activation of a developmental transcription factor in Bacillus subtilis

Cited by 87 publications

References 49 publications

Compartmentalization of Gene Expression duringBacillus subtilisSpore Formation

Compartmentalization of Gene Expression duringBacillus subtilisSpore Formation

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

BofA protein inhibits intramembrane proteolysis of pro-σKin an intercompartmental signaling pathway duringBacillus subtilissporulation

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

BofA protein inhibits intramembrane proteolysis of pro-σ^Kin an intercompartmental signaling pathway duringBacillus subtilissporulation