The spo0K locus of Bacillus subtilis is homologous to the oligopeptide permease locus and is required for sporulation and competence

Rudner, David Z.; LeDeaux, John R.; Ireton, Keith; Grossman, Alan D.

doi:10.1128/jb.173.4.1388-1398.1991

Cited by 233 publications

(230 citation statements)

References 54 publications

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“…E. coli cells were made competent and transformed by standard procedures (27). Cells of B. subtilis were made competent as previously described (6,26).…”

Section: Methodsmentioning

confidence: 99%

Characterization of csh203::Tn917lac, a mutation in Bacillus subtilis that makes the sporulation sigma factor sigma-H essential for normal vegetative growth

Hicks

Grossman

1995

J Bacteriol

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spo0H encodes a sigma factor, sigma-H, of RNA polymerase that is required for sporulation in Bacillus subtilis. Null mutations in spo0H block the initiation of sporulation but have no obvious effect on vegetative growth. We have characterized an insertion mutation, csh203::Tn917lac, that makes spo0H essential for normal growth. In otherwise wild-type cells, the csh203::Tn917lac insertion mutation has no obvious effect on cell growth, viability, or sporulation. However, in combination with a mutation in spo0H, the csh203 mutation causes a defect in vegetative growth. The csh203::Tn917lac insertion mutation was found to be located within orf23, the first gene of the rpoD (sigma-A) operon. The transposon insertion separates the major vegetative promoters P1 and P2 from the coding regions of two essential genes, dnaG (encoding DNA primase) and rpoD (encoding the major sigma factor, sigma-A) and leaves these genes under the control of minor promoters, including P4, a promoter controlled by sigma-H. The csh203 insertion mutation caused a 2-to 10-fold increase in expression of promoters recognized by RNA polymerase containing sigma-H. The increased expression of genes controlled by sigma-H in the csh203 single mutant, as well as the growth defect of the csh203 spo0H double mutant, was due to effects on rpoD and not to a defect in orf23 or dnaG.

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“…E. coli cells were made competent and transformed by standard procedures (27). Cells of B. subtilis were made competent as previously described (6,26).…”

Section: Methodsmentioning

confidence: 99%

Characterization of csh203::Tn917lac, a mutation in Bacillus subtilis that makes the sporulation sigma factor sigma-H essential for normal vegetative growth

Hicks

Grossman

1995

J Bacteriol

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“…The small Phr precursor peptides are cleaved and secreted from the cell, and at least some of them accumulate in the culture supernatant (2). They are subsequently imported by Opp oligopeptide permeases into the cytoplasm where the Phr derived pentapeptides (PEP5) intracellularly inhibit the activity of their cognate Raps (3)(4)(5). Thus, PEP5s can be indicators of cell density and have been implied in facilitating cell-cell communication (2,(5)(6)(7)(8).…”

mentioning

confidence: 99%

Complexity in bacterial cell–cell communication: Quorum signal integration and subpopulation signaling in the Bacillus subtilis phosphorelay

Bischofs

Hug²,

Liu³

et al. 2009

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

102

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A common form of quorum sensing in Gram-positive bacteria is mediated by peptides that act as phosphatase regulators (Phr) of receptor aspartyl phosphatases (Raps). In Bacillus subtilis, several Phr signals are integrated in sporulation phosphorelay signal transduction. We theoretically demonstrate that the phosphorelay can act as a computational machine performing a sensitive division operation of kinase-encoded signals by quorum-modulated Rap signals, indicative of cells computing a ''food per cell'' estimate to decide whether to enter sporulation. We predict expression from the rapA-phrA operon to bifurcate as relative environmental signals change in a developing population. We experimentally observe that the rapA-phrA operon is heterogeneously induced in sporulating microcolonies. Uninduced cells sporulate rather synchronously early on, whereas the RapA/PhrA subpopulation sporulates less synchronously throughout later stationary phase. Moreover, we show that cells sustain PhrA expression during periods of active growth. Together with the model, these findings suggest that the phosphorelay may normalize environmental signals by the size of the (sub)population actively competing for nutrients (as signaled by PhrA). Generalizing this concept, the various Phrs could facilitate subpopulation communication in dense isogenic communities to control the physiological strategies followed by differentiated subpopulations by interpreting (environmental) signals based on the spatiotemporal community structure.heterogeneity ͉ Phr ͉ quorum sensing ͉ sporulation ͉ model

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“…Pre-Phr peptides are exported and cleaved to form the mature Phr pentapeptides (Lazazzera, 2001;Perego and Brannigan, 2001). The oligopeptide permease (Opp), an ATP-binding cassette (ABC) transporter that imports small peptides (Perego et al, 1991;Rudner et al, 1991), transports the Phr peptides into the cell, where they can inhibit the activities of Rap proteins (Lazazzera et al, 1997;Perego, 1997).…”

Section: Microbially Synthesized Bioactive Peptides By the Genus Bacimentioning

confidence: 99%

Proteome-wide analysis of the functional roles of bacilysin biosynthesis in Bacillus subtilis

Özcengiz¹,

Taşkin

Demir³

et al. 2014

New Biotechnology

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The spo0K locus of Bacillus subtilis is homologous to the oligopeptide permease locus and is required for sporulation and competence

Cited by 233 publications

References 54 publications

Characterization of csh203::Tn917lac, a mutation in Bacillus subtilis that makes the sporulation sigma factor sigma-H essential for normal vegetative growth

Characterization of csh203::Tn917lac, a mutation in Bacillus subtilis that makes the sporulation sigma factor sigma-H essential for normal vegetative growth

Complexity in bacterial cell–cell communication: Quorum signal integration and subpopulation signaling in the Bacillus subtilis phosphorelay

Proteome-wide analysis of the functional roles of bacilysin biosynthesis in Bacillus subtilis

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