Identification of target promoters for the Bacillus subtilis σ X factor using a consensus-directed search 1 1Edited by R. Ebright

Huang, Xuejun; Helmann, John D.

doi:10.1006/jmbi.1998.1765

Cited by 106 publications

(160 citation statements)

References 24 publications

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“…RNA was either purified from in vitro runoff transcription reaction mixtures or extracted from late-log-phase B. subtilis cells using phenol-chloroform extraction as described previously (22). A PCR fragment a The first gene in each known or putative X -dependent operon and its ( X -dependent) promoter region are listed.…”

Section: Methodsmentioning

confidence: 99%

“…Previously, saturation mutagenesis of the sigX autoregulatory promoter was used to identify those bases important for Xdependent promoter recognition. The resulting consensus was used to search the partially sequenced B. subtilis genome (63% complete at the time the analysis was done [22]) to identify candidate promoters. While this approach identified several X target genes, others were subsequently found to be primarily controlled by W or M , which recognize promoters with closely related sequences (22,35).…”

Section: Defining Thementioning

confidence: 99%

“…Interestingly, most X -controlled genes are also transcribed by other forms of holoenzyme. For example, csbB has an additional B -dependent promoter, lytR and rapD both have additional A -dependent promoters, and sigX itself is preferentially transcribed from an upstream A -dependent site in addition to the X -dependent autoregulatory promoter (20,22). Moreover, in some cases (e.g., abh and divIC) the promoter activated by the E X holoenzyme can also be recognized by the E W holoenzyme at least in vitro (21).…”

mentioning

confidence: 99%

“…To understand the function of X , we identified several X -regulated genes using a consensus promoter search method (22). In these initial studies, we characterized six genes that are preceded by promoters recognized by X : sigX, abh (an AbrB homolog), csbB (a membrane-bound glucosyl transferase) (2), divIC (a membrane-bound cell-division initiation protein), lytR (a negative regulator of autolysin) (30), and rapD (a response regulator aspartate phosphatase) (43).…”

mentioning

confidence: 99%

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The Bacillus subtilis Extracytoplasmic-Function σ ^X Factor Regulates Modification of the Cell Envelope and Resistance to Cationic Antimicrobial Peptides

2004

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Bacillus subtilis contains seven extracytoplasmic-function factors that activate partially overlapping regulons. We here identify four additional members of the X regulon, pbpX (penicillin-binding protein), ywnJ, the dlt operon (D-alanylation of teichoic acids), and the pss ybfM psd operon (phosphatidylethanolamine biosynthesis). Modification of teichoic acids by esterification with D-alanine and incorporation of phosphatidylethanolamine into the cell membrane have a common consequence: in both cases positively charged amino groups are introduced into the cell envelope. The resulting reduction in the net negative charge of the cell envelope has been previously implicated as a resistance mechanism specific for cationic antimicrobial peptides. Consistent with this notion, we find that both sigX and dltA mutants are more sensitive to nisin than wild-type cells. We conclude that activation of the X regulon serves to alter cell surface properties to provide protection against antimicrobial peptides.Bacillus subtilis encodes seven extracytoplasmic-function (ECF) factors. Most studies to date have focused on three:X , W , and M (reviewed in reference 19). sigX and its downstream gene rsiX (encoding the anti-X factor) were originally observed to be homologous (but not orthologous) to Escherichia coli fecI and fecR, which are involved in expression of ferric citrate transport genes (37). Although expression of sigX in E. coli can complement a fecI mutant (4), the B. subtilis sigX mutant is not affected in any known ferri-siderophore uptake systems (20).To understand the function of X , we identified several X -regulated genes using a consensus promoter search method (22). In these initial studies, we characterized six genes that are preceded by promoters recognized by X : sigX, abh (an AbrB homolog), csbB (a membrane-bound glucosyl transferase) (2), divIC (a membrane-bound cell-division initiation protein), lytR (a negative regulator of autolysin) (30), and rapD (a response regulator aspartate phosphatase) (43). These results suggested that X modulates aspects of cell envelope metabolism. Interestingly, most X -controlled genes are also transcribed by other forms of holoenzyme. For example, csbB has an additional B -dependent promoter, lytR and rapD both have additional A -dependent promoters, and sigX itself is preferentially transcribed from an upstream A -dependent site in addition to the X -dependent autoregulatory promoter (20,22). Moreover, in some cases (e.g., abh and divIC) the promoter activated by the E X holoenzyme can also be recognized by the E W holoenzyme at least in vitro (21). Similarly, the recently defined bcrC gene (a bacitracin resistance gene) is transcribed from a promoter that is recognized by either X or M (7, 38). The unknown function of many X -controlled genes makes it difficult to predict a phenotype for the sigX mutant. This challenge is exacerbated by the fact that many of the genes are expressed from multiple promoters or by multiple holoenzyme forms activating the same promoter. The latte...

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Section: Methodsmentioning

confidence: 99%

Section: Defining Thementioning

confidence: 99%

mentioning

confidence: 99%

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The Bacillus subtilis Extracytoplasmic-Function σ ^X Factor Regulates Modification of the Cell Envelope and Resistance to Cationic Antimicrobial Peptides

2004

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“…pbpX is part of the s X regulon, which is thought to modulate aspects of cell envelope metabolism, possibly through regulation of cell-surface modification (Cao & Helmann, 2004;Huang & Helmann, 1998). A sigX-null mutant is impaired in its ability to survive at high temperature (Huang et al, 1997).…”

Section: Pbp2c Pbp2d and Pbpx Localize To The Presporementioning

confidence: 99%

Dynamic localization of penicillin-binding proteins during spore development in Bacillus subtilis

Scheffers

2005

Microbiology

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During Bacillus subtilis spore formation, many membrane proteins that function in spore development localize to the prespore septum and, subsequently, to the outer prespore membrane. Recently, it was shown that the cell-division-specific penicillin-binding proteins (PBPs) 1 and 2b localize to the asymmetric prespore septum. Here, the author studied the localization of other PBPs, fused to green fluorescent protein (GFP), during spore formation. Fusions to PBPs 4, 2c, 2d, 2a, 3, H, 4b, 5, 4a, 4* and X were expressed during vegetative growth, and their localization was monitored during sporulation. Of these PBPs, 2c, 2d, 4b and 4* have been implicated as having a function in sporulation. It was found that PBP2c, 2d and X changed their localization, while the other PBPs tested were not affected. The putative endopeptidase PbpX appears to spiral out in a pattern that resembles FtsZ redistribution during sporulation, but a pbpX knockout strain had no distinguishable phenotype. PBP2c and 2d localize to the prespore septum and follow the membrane during engulfment, and so are redistributed to the prespore membrane. A similar pattern was observed when GFP-PBP2c was expressed in the mother cell from a sporulation-specific promoter. This work shows that various PBPs known to function during sporulation are redistributed from the cytoplasmic membrane to the prespore.

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Defining the Bacillus subtilis σW regulon: a comparative analysis of promoter consensus search, run-off transcription/macroarray analysis (ROMA), and transcriptional profiling approaches

Cao

Kobel

Morshedi

et al. 2002

Journal of Molecular Biology

179

204

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Identification of target promoters for the Bacillus subtilis σ X factor using a consensus-directed search 1 1Edited by R. Ebright

Cited by 106 publications

References 24 publications

The Bacillus subtilis Extracytoplasmic-Function σ ^X Factor Regulates Modification of the Cell Envelope and Resistance to Cationic Antimicrobial Peptides

The Bacillus subtilis Extracytoplasmic-Function σ ^X Factor Regulates Modification of the Cell Envelope and Resistance to Cationic Antimicrobial Peptides

Dynamic localization of penicillin-binding proteins during spore development in Bacillus subtilis

Defining the Bacillus subtilis σW regulon: a comparative analysis of promoter consensus search, run-off transcription/macroarray analysis (ROMA), and transcriptional profiling approaches

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Identification of target promoters for the Bacillus subtilis σ X factor using a consensus-directed search 1 1Edited by R. Ebright

Cited by 106 publications

References 24 publications

The Bacillus subtilis Extracytoplasmic-Function σ X Factor Regulates Modification of the Cell Envelope and Resistance to Cationic Antimicrobial Peptides

The Bacillus subtilis Extracytoplasmic-Function σ X Factor Regulates Modification of the Cell Envelope and Resistance to Cationic Antimicrobial Peptides

Dynamic localization of penicillin-binding proteins during spore development in Bacillus subtilis

Defining the Bacillus subtilis σW regulon: a comparative analysis of promoter consensus search, run-off transcription/macroarray analysis (ROMA), and transcriptional profiling approaches

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The Bacillus subtilis Extracytoplasmic-Function σ ^X Factor Regulates Modification of the Cell Envelope and Resistance to Cationic Antimicrobial Peptides

The Bacillus subtilis Extracytoplasmic-Function σ ^X Factor Regulates Modification of the Cell Envelope and Resistance to Cationic Antimicrobial Peptides