SpoIIB Localizes to Active Sites of Septal Biogenesis and Spatially Regulates Septal Thinning during Engulfment in
            <i>Bacillus subtilis</i>

Pérez, Ana Rosa; Mello, Angelica Abanes-De; Pogliano, Kit

doi:10.1128/jb.182.4.1096-1108.2000

Cited by 62 publications

(102 citation statements)

References 54 publications

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“…It later became clear that it is only required in strains in which a second gene expressed in the predivisional cell, spoVG (319), has been disrupted (190). Single mutations in either spoIIB and spoVG cause a very mild defect, whereas the double mutant displays little autolysis and sporulates poorly (190,224). SpoIIB localizes to the asymmetric septum and bears weak homology with an amidase, suggesting a direct role in engulfment (190,224).…”

Section: Initiation Of Engulfmentmentioning

confidence: 99%

“…Single mutations in either spoIIB and spoVG cause a very mild defect, whereas the double mutant displays little autolysis and sporulates poorly (190,224). SpoIIB localizes to the asymmetric septum and bears weak homology with an amidase, suggesting a direct role in engulfment (190,224). The function of SpoVG in engulfment is unclear; it appears to play some role in inhibiting asymmetric division (195,224).…”

Section: Initiation Of Engulfmentmentioning

confidence: 99%

“…spoIIQ mutants display a block just prior to completion of engulfment (178). Loci expressed before septation are also involved in engulfment (a spoIIB spoVG double mutant displays aberrant septal wall autolysis) (190,224), and the spoIIIE locus has been shown to be required for the membrane fusion event (264,266).…”

Section: Initiation Of Engulfmentmentioning

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: Initiation Of Engulfmentmentioning

confidence: 99%

Section: Initiation Of Engulfmentmentioning

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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“…This peptide was chosen for its hydrophilicity and corresponds to amino acids 104 -123 of SpoIIIAH plus an N-terminal Cys for conjugation to KLH. Immunofluorescence microscopy was performed as described (34).…”

Section: Co-immunoprecipitation and Westernmentioning

confidence: 99%

Impact of Membrane Fusion and Proteolysis on SpoIIQ Dynamics and Interaction with SpoIIIAH

Chiba¹,

Coleman

Pogliano

2007

Journal of Biological Chemistry

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The onset of engulfment-dependent gene expression during Bacillus subtilis sporulation requires the forespore membrane protein SpoIIQ, which recruits mother cell proteins involved in late gene expression to the outer forespore membrane. Engulfment activates the late forespore transcription factor G , which produces high levels of the secreted SpoIVB protease that is required for activation of the late mother cell transcription factor K . Engulfment also triggers the proteolytic cleavage of SpoIIQ, an event that depends on the SpoIVB protease but not on G activity. To determine if SpoIVB directly cleaves SpoIIQ and to determine if this event participates in the onset of late gene expression, we purified SpoIVB, SpoIIQ, and SpoIVFA (another SpoIVB substrate). SpoIVB directly cleaved SpoIIQ at the same site in vitro and in vivo and cleaved SpoIVFA in at least three different locations. SpoIIQ cleavage depends on membrane fusion, but not on G activity, suggesting that the ability of SpoIVB to cleave substrates is regulated by membrane fusion. We isolated SpoIVB-resistant SpoIIQ proteins by random mutagenesis of codons at the cleavage site and demonstrated that SpoIIQ processing is dispensable for spore formation and for activation of late forespore and mother cell gene expression. Fluorescence recovery after photobleaching analysis demonstrated that membrane fusion releases SpoIIQ from an immobile complex, an event that could allow SpoIVB to cleave SpoIIQ. We propose that this membrane fusion-dependent reorganization in the complex, rather than SpoIIQ proteolysis itself, is necessary for the onset of late transcription.Endospore formation in Bacillus subtilis and its relatives depends on engulfment, a phagocytosis-like process that mediates a dramatic rearrangement of the sporangium from two adjacent daughter cells, to an endospore in which the forespore lies within the cytoplasm of the larger mother cell (see Fig. 1; reviewed by Refs. 1 and 2). Engulfment is critical for sporulation, because it allows spore assembly to occur in a protected environment. It also serves as a morphological checkpoint for activation of the late forespore and mother cell transcription factors G and K , respectively (reviewed by Refs. 1-4). The endospore-forming bacteria must therefore have some mechanism to sense the completion of engulfment and to couple this morphological event to the onset of late gene expression.The forespore transcription factor G is the first to become active after engulfment, but it remains unclear how G is held inactive during engulfment or activated after engulfment. More is known about the regulation of the second late transcription factor, K , which becomes active in the mother cell (summarized in Fig. 1B and reviewed by Refs. 1-4). The K factor is initially synthesized as an inactive pro-protein containing a hydrophobic leader sequence, which functions as a covalently attached anti-sigma factor (5). This leader sequence is removed by the intramembrane protease SpoIVFB, which cleaves pro-K within the membrane ...

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“…TipN and TipF in Caulobacter crescentus and SpoIIB in Bacillus subtilis are recruited to the midcell before division and are positioned at the poles after septation is complete (8)(9)(10). Other proteins appear to respond to cell morphology and become localized at the poles and septa (e.g., the cell division sites) of rod-shaped bacteria where they participate in a variety of physiological processes, including division, spore formation, chemotaxis, and cell-wall remodeling (5).…”

mentioning

confidence: 99%

Cardiolipin microdomains localize to negatively curved regions of Escherichia coli membranes

Renner¹,

Weibel

2011

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

309

336

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Many proteins reside at the cell poles in rod-shaped bacteria. Several hypotheses have drawn a connection between protein localization and the large cell-wall curvature at the poles. One hypothesis has centered on the formation of microdomains of the lipid cardiolipin (CL), its localization to regions of high membrane curvature, and its interaction with membrane-associated proteins. A lack of experimental techniques has left this hypothesis unanswered. This paper describes a microtechnology-based technique for manipulating bacterial membrane curvature and quantitatively measuring its effect on the localization of CL and proteins in cells. We confined Escherichia coli spheroplasts in microchambers with defined shapes that were embossed into a layer of polymer and observed that the shape of the membrane deformed predictably to accommodate the walls of the microchambers. Combining this technique with epifluorescence microscopy and quantitative image analyses, we characterized the localization of CL microdomains in response to E. coli membrane curvature. CL microdomains localized to regions of high intrinsic negative curvature imposed by microchambers. We expressed a chimera of yellow fluorescent protein fused to the N-terminal region of MinD-a spatial determinant of E. coli division plane assembly-in spheroplasts and observed its colocalization with CL to regions of large, negative membrane curvature. Interestingly, the distribution of MinD was similar in spheroplasts derived from a CL synthase knockout strain. These studies demonstrate the curvature dependence of CL in membranes and test whether these structures participate in the localization of MinD to regions of negative curvature in cells.A central question in cell biology is how the spatial organization of proteins and lipids is established, maintained, and replicated and how it fluctuates in response to external stimuli. Eukaryotic cells use several mechanisms to accomplish this task, including a dynamic cytoskeleton that controls the spatial and temporal position of proteins, nucleic acid, and organelles (1). The formation of lipid microdomains in the membrane also is involved in the localization of integral membrane proteins (2). These mechanisms play a critical role in cell physiology and behavior.Bacteria also use mechanisms for controlling the intracellular location of proteins, lipids, and nucleic acid. The persistent historical view of bacterial cells as lacking spatial control over their intracellular components inhibited the field. Bacteria are sophisticated organisms that use tightly regulated physiological mechanisms similar to many of those used by eukaryotic cells, including controlling shape, regulating growth and division, transporting intracellular components (e.g., proteins, plasmids, DNA, and RNA), and polarizing the cell (3, 4). These organisms have several remarkable structural characteristics, but one of the most fundamental questions in this area of microbiology-how cells produce, maintain, and replicate their spatial organization-still...

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SpoIIB Localizes to Active Sites of Septal Biogenesis and Spatially Regulates Septal Thinning during Engulfment in Bacillus subtilis

Cited by 62 publications

References 54 publications

Compartmentalization of Gene Expression duringBacillus subtilisSpore Formation

Compartmentalization of Gene Expression duringBacillus subtilisSpore Formation

Impact of Membrane Fusion and Proteolysis on SpoIIQ Dynamics and Interaction with SpoIIIAH

Cardiolipin microdomains localize to negatively curved regions of Escherichia coli membranes

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