Cell-cell signaling pathway activating a developmental transcription factor in Bacillus subtilis.

Londoño-Vallejo, J. Arturo; Stragier, Patrick

doi:10.1101/gad.9.4.503

Cited by 123 publications

(152 citation statements)

References 27 publications

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“…twofold by disruption of spoIIGB, the gene encoding E , and was unaffected by disruption of spoIIIG, the gene encoding G . This genetic dependency as well as the timing of expression is identical to the one exhibited by spoIIR (Karow et al, 1995;Londoño-Vallejo and Stragier, 1995). However, the level of accumulated ␤-galactosidase reached approx.…”

Section: Expression Of the Spoiiq Genesupporting

confidence: 64%

“…In the course of our search for the spoIIR gene we screened a B. subtilis integrative plasmid library creating chromosomal transcriptional fusions to the Escherichia coli lacZ gene (O'Reilly et al, 1994) and we used a genetic background that allowed us to identify, on plates, lacZ fusions expressed from F -dependent promoters (Londoño-Vallejo and Stragier, 1995). Nine different loci were characterized as being controlled by F and the corresponding plasmids were rescued from the chromosome.…”

Section: Identification Of the Spoiiq Genementioning

confidence: 99%

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spoIIQ, a forespore‐expressed gene required for engulfment in Bacillus subtilis

Fréhel

Stragier

1997

Molecular Microbiology

131

135

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SummaryA crucial step in converting an actively growing Bacillus subtilis cell into a dormant spore is the formation of a cell within a cell. This unusual structure is created by a phagocytosis-like process in which the larger mother cell progressively engulfs the adjacent smaller forespore. Only mutations blocking engulfment at an early stage and affecting genes expressed in the mother cell have been identified. Here we describe a new locus, spoIIQ, which is transcribed in the forespore and which encodes a membrane-bound protein required at a late stage of engulfment. Immunofluorescence microscopy analysis have shown that SpoIIQ is initially targeted to the septum at the boundary between the two cells and then spreads around the entire membrane of the forespore. Septum targeting requires only the first 52 residues of SpoIIQ as well as unidentified forespore-specific components. Electron-microscopy studies of cells engineered to activate the mother-cell program of gene expression independently of the forespore indicate that other as yet uncharacterized genes are involved in engulfment and that this morphological process is driven from both sides of the forespore envelope.

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Section: Expression Of the Spoiiq Genesupporting

confidence: 64%

Section: Identification Of the Spoiiq Genementioning

confidence: 99%

spoIIQ, a forespore‐expressed gene required for engulfment in Bacillus subtilis

Fréhel

Stragier

1997

Molecular Microbiology

131

135

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“…transcription from the cse15 and cse60 promoters commenced around h 2 of sporulation whereas utilization of the csk22 promoter was not detected before the 4th h. The temporal pattern of expression detected for cse15 and cse60 is that observed for many E -controlled genes (20,44,47). E is activated in the mother cell (19,34,43,44) and is functional in this sporangial compartment until at least the end of the engulfment sequence (20,45,48).…”

Section: Discussionmentioning

confidence: 99%

“…The activation of the different sigma factors is itself strongly coupled to specific points in the morphological sequence (45). E , for example, is synthesized in a pro-form in the predivisional cell (32,42), and its proteolytic activation is somehow coupled to the septation process and to the activity of F , a prespore-specific sigma factor (35,44). 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).…”

mentioning

confidence: 99%

“…E , for example, is synthesized in a pro-form in the predivisional cell (32,42), and its proteolytic activation is somehow coupled to the septation process and to the activity of F , a prespore-specific sigma factor (35,44). 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).…”

mentioning

confidence: 99%

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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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