Gene encoding a morphogenic protein required in the assembly of the outer coat of the Bacillus subtilis endospore.

Zheng, Liyun; Donovan, William P.; Fitz-James, Philip C.; Losick, Richard

doi:10.1101/gad.2.8.1047

Cited by 201 publications

(284 citation statements)

References 18 publications

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“…The spoIID, spoIIM and spoIIP genes are essential for the engulfment process, and also act to prevent a second polar division of the sporulating cell (Abanes-De Mello et al, 2002;Eichenberger et al, 2001;Frandsen & Stragier, 1995;Lopez-Diaz et al, 1986;Pogliano et al, 1999;Rong et al, 1986;. The initial stages in assembly of the spore coat require expression of the spoIVA, cotE, spoVID and safA genes, whose products are morphogenetic proteins which guide the assembly of the several coat structural components (Beall et al, 1993;Driks et al, 1994;Ozin et al, 2000;Takamatsu et al, 1999;Zheng et al, 1988), and several genes which encode spore coat components with no obvious morphogenetic functions are also under the control of s E (e.g. Henriques et al, 1995); spoVE, spoVD, dacB, spoVR, spmAB and murF (Supplementary Table S2), among others, are required for synthesis or modification of the spore cortex peptidoglycan Daniel et al, 1994;Henriques et al, 1992;Popham et al, 1995).…”

Section: Differentiation Of the Compartment-specific Sporulation Regumentioning

confidence: 99%

Genome-wide analysis of temporally regulated and compartment-specific gene expression in sporulating cells of Bacillus subtilis

et al. 2005

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Temporal and compartment-specific control of gene expression during sporulation in Bacillus subtilis is governed by a cascade of four RNA polymerase subunits. s F in the prespore and s E in the mother cell control early stages of development, and are replaced at later stages by s G and s K , respectively. Ultimately, a comprehensive description of the molecular mechanisms underlying spore morphogenesis requires the knowledge of all the intervening genes and their assignment to specific regulons. Here, in an extension of earlier work, DNA macroarrays have been used, and members of the four compartment-specific sporulation regulons have been identified. Genes were identified and grouped based on: i) their temporal expression profile and ii) the use of mutants for each of the four sigma factors and a bofA allele, which allows s K activation in the absence of s G . As a further test, artificial production of active alleles of the sigma factors in non-sporulating cells was employed. A total of 439 genes were found, including previously characterized genes whose transcription is induced during sporulation: 55 in the s F regulon, 154 s E -governed genes, 113 s G -dependent genes, and 132 genes under s K control. The results strengthen the view that the activities of s F , s E , s G and s K are largely compartmentalized, both temporally as well as spatially, and that the major vegetative sigma factor (s A ) is active throughout sporulation. The results provide a dynamic picture of the changes in the overall pattern of gene expression in the two compartments of the sporulating cell, and offer insight into the roles of the prespore and the mother cell at different times of spore morphogenesis.

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Section: Differentiation Of the Compartment-specific Sporulation Regumentioning

confidence: 99%

Genome-wide analysis of temporally regulated and compartment-specific gene expression in sporulating cells of Bacillus subtilis

et al. 2005

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“…Rather, CotF is present as two proteolytic fragments of 8 and 5 kDa, and CotT is present as a proteolytic fragment of 8 kDa (2,4). Coat proteins are organized in two principal layers, a lamellar inner coat and an electron-dense outer coat (1), with certain proteins, such as CotD, being present in the inner coat, and other proteins, such as CotA, CotB, and CotC, being present in the outer coat (31). The coat is assembled at intermediate to late stages of sporulation when the nascent spore (known as the forespore) is present as a free protoplast, wholly engulfed within the mother cell compartment of the developing sporangium.…”

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confidence: 99%

“…The CotE ring is separated from the outer surface of the forespore (where SpoIVA is located) by a small gap, which is believed to be the site at which the inner coat will be assembled. Meanwhile, CotE dictates the assembly of the proteins of the outer coat, where it is itself located (8,31). The production of coat proteins is governed by a hierarchical regulatory cascade of four transcription factors acting in the mother cell compartment of the sporangium in the sequence E SpoIIID K GerE (33).…”

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confidence: 99%

“…So far, genes for 10 of these coat proteins have been identified. These are located at diverse positions on the chromosome and encode polypeptides of 65 (CotA), 59 (CotB), 10 (CotC), 9 (CotD), 24 (CotE), 19 (CotF), 10 (CotT), 19 (CotX), 26 (CotY), and 18 (CotZ) kDa (2,4,7,29,31). In the cases of CotF and CotT, little of the full-length gene products is found in the coat.…”

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confidence: 99%

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An additional GerE-controlled gene encoding an abundant spore coat protein from Bacillus subtilis

et al. 1995

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We describe the identification and characterization of a gene, herein designated cotG, encoding an abundant coat protein from the spores of Bacillus subtilis. The cotG open reading frame is 195 codons in length and is capable of encoding a polypeptide of 24 kDa that contains nine tandem copies of the 13-amino-acid long, approximately repeated sequence H/Y-K-K-S-Y-R/C-S/T-H/Y-K-K-S-R-S.cotG is located at 300؇ on the genetic map close to another coat protein gene, cotB. The cotG and cotB genes are in divergent orientation and are separated by 1.3 kb. Like the promoter for cotB, the cotG promoter is induced at a late stage of sporulation under the control of the RNA polymerase sigma factor K and the DNA-binding protein GerE. The ؊10 and ؊35 nucleotide sequences of the cotG promoter resemble those of other promoters recognized by K -containing RNA polymerase, and centered 70 bp upstream of the apparent start site is a sequence that matches the consensus binding site for GerE. Spore coat proteins from a newly constructed cotG null mutant lack not only CotG but also CotB, a finding that suggests that CotG may be a morphogenetic protein that is required for the incorporation of CotB into the coat.Spores of the gram-positive bacterium Bacillus subtilis are encased in a complex protein shell known as the coat consisting of 15 or more different proteins. So far, genes for 10 of these coat proteins have been identified. These are located at diverse positions on the chromosome and encode polypeptides of 65 (CotA), 59 (CotB), 10 (CotC), 9 (CotD), 24 (CotE), 19 (CotF), 10 (CotT), 19 (CotX), 26 (CotY), and 18 (CotZ) kDa (2,4,7,29,31). In the cases of CotF and CotT, little of the full-length gene products is found in the coat. Rather, CotF is present as two proteolytic fragments of 8 and 5 kDa, and CotT is present as a proteolytic fragment of 8 kDa (2, 4). Coat proteins are organized in two principal layers, a lamellar inner coat and an electron-dense outer coat (1), with certain proteins, such as CotD, being present in the inner coat, and other proteins, such as CotA, CotB, and CotC, being present in the outer coat (31). The coat is assembled at intermediate to late stages of sporulation when the nascent spore (known as the forespore) is present as a free protoplast, wholly engulfed within the mother cell compartment of the developing sporangium. Coat proteins are recruited to the outer surface of the membrane surrounding the forespore by the sporulation protein SpoIVA (which has not been detected in mature spores and hence is not referred to as a coat protein) (8,19,21). Morphogenetic events under the control of SpoIVA lead to the assembly of a ring of CotE protein around the forespore (8). The CotE ring is separated from the outer surface of the forespore (where SpoIVA is located) by a small gap, which is believed to be the site at which the inner coat will be assembled. Meanwhile, CotE dictates the assembly of the proteins of the outer coat, where it is itself located (8, 31). The production of coat proteins is governed by ...

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“…Conversion of pro-E to its active form, E , which occurs exclusively in the mother cell, inaugurates the program of gene expression in this compartment (19,35,44,68). The E form of RNA polymerase (E E ) directs the transcription of a heterogeneous group of genes controlling functions as diverse as engulfment (23,56,58,62), germination (49,70), cortex synthesis (2,9,14,43,52,54,60,64), and coat morphogenesis (3,18,28,49,54,60,70), as well as genes that may assist in the control of the metabolic state of the mother cell (7,8,26,37). E E also drives expression of at least two regulatory genes, spoIIID (40,62,68) and sigK (39,68).…”

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confidence: 99%

cse15, cse60, and csk22 are new members of mother-cell-specific sporulation regulons in Bacillus subtilis

et al. 1997

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We report on the characterization of three new transcription units expressed during sporulation in Bacillus subtilis. Two of the units, cse15 and cse60, were mapped at about 123؇ and 62؇ on the genetic map, respectively. Their transcription commenced around h 2 of sporulation and showed an absolute requirement for E . Maximal expression of both cse15 and cse60 further depended on the DNA-binding protein SpoIIID. Primer extension results revealed ؊10 and ؊35 sequences upstream of the cse15 and cse60 coding sequences very similar to those utilized by E -containing RNA polymerase. Alignment of these and other regulatory regions led to a revised consensus sequence for E -dependent promoters. A third transcriptional unit, designated csk22, was localized at approximately 173؇ on the chromosome. Transcription of csk22 was activated at h 4 of sporulation, required the late mother-cell regulator K , and was repressed by the GerE protein. Sequences in the csk22 promoter region were similar to those of other K -dependent promoters. The cse60 locus was deduced to encode an acidic product of only 60 residues. A 37.6-kDa protein apparently encoded by cse15 was weakly related to the heavy chain of myosins, as well as to other myosin-like proteins, and is predicted to contain a central, 100 residue-long coiled-coil domain. Finally, csk22 is inferred to encode a 18.2-kDa hydrophobic product with five possible membrane-spanning helices, which could function as a transporter.

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Gene encoding a morphogenic protein required in the assembly of the outer coat of the Bacillus subtilis endospore.

Cited by 201 publications

References 18 publications

Genome-wide analysis of temporally regulated and compartment-specific gene expression in sporulating cells of Bacillus subtilis

Genome-wide analysis of temporally regulated and compartment-specific gene expression in sporulating cells of Bacillus subtilis

An additional GerE-controlled gene encoding an abundant spore coat protein from Bacillus subtilis

cse15, cse60, and csk22 are new members of mother-cell-specific sporulation regulons in Bacillus subtilis

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