Isolation and characterization of csbB, a gene controlled by Bacillus subtilis general stress transcription factor σB

Akbar, Samina; Price, Chester W.

doi:10.1016/0378-1119(96)00287-9

Cited by 26 publications

(17 citation statements)

References 23 publications

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“…The linkage between Cnm and PgfS is somewhat unexpected given that pgfS, unlike cnm, is part of the core genome of S. mutans (35). A PgfS homolog, termed CsbB, was first described for Bacillus subtilis (36). In B. subtilis, csbB expression is controlled by the alternative B factor and is predicted to participate in cell envelope biogenesis (36).…”

Section: Discussionmentioning

confidence: 99%

“…A PgfS homolog, termed CsbB, was first described for Bacillus subtilis (36). In B. subtilis, csbB expression is controlled by the alternative B factor and is predicted to participate in cell envelope biogenesis (36). Although the genomes of streptococcal species lack the B factor, the link between PgfS and cell envelope biogenesis in S. mutans remains to be determined.…”

Section: Discussionmentioning

confidence: 99%

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Modification of Streptococcus mutans Cnm by PgfS Contributes to Adhesion, Endothelial Cell Invasion, and Virulence

et al. 2014

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Expression of the surface protein Cnm has been directly implicated in the ability of certain strains of Streptococcus mutans to bind to collagen and to invade human coronary artery endothelial cells (HCAEC) and in the killing of Galleria mellonella. Sequencing analysis of Cnm ؉ strains revealed that cnm is located between the core genes SMU.2067 and SMU.2069. Reverse transcription-PCR (RT-PCR) analysis showed that cnm is cotranscribed with SMU.2067, encoding a putative glycosyltransferase referred to here as PgfS (protein glycosyltransferase of streptococci). Notably, Cnm contains a threonine-rich domain predicted to undergo O-linked glycosylation. The previously shown abnormal migration pattern of Cnm, the presence of the threonine-rich domain, and the molecular linkage of cnm with pgfS lead us to hypothesize that PgfS modifies Cnm. A ⌬pgfS strain showed defects in several traits associated with Cnm expression, including collagen binding, HCAEC invasion, and killing of G. mellonella. Western blot analysis revealed that Cnm from the ⌬pgfS mutant migrated at a lower molecular weight than that from the parent strain. In addition, Cnm produced by ⌬pgfS was highly susceptible to proteinase K degradation, in contrast to the high-molecular-weight Cnm version found in the parent strain. Lectin-binding analyses confirmed the glycosylated nature of Cnm and strongly suggested the presence of N-acetylglucosamine residues attached to Cnm. Based on these findings, the phenotypes observed in ⌬pgfS are most likely associated with defects in Cnm glycosylation that affects protein function, stability, or both. In conclusion, this study demonstrates that Cnm is a glycoprotein and that posttranslational modification mediated by PgfS contributes to the virulence-associated phenotypes linked to Cnm.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Modification of Streptococcus mutans Cnm by PgfS Contributes to Adhesion, Endothelial Cell Invasion, and Virulence

et al. 2014

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“…The second group of stimuli includes physical stress-factors such as heat-, salt-, and acid-stress, but not oxidative-stress . This group of stimuli induces the synthesis of s B via a two-component system of RsbS and RsbT that changes the balance of a complex network of antisigma (RsbW) factor and its agonist (non-phosphorylated RsbV) to activate s B (Akbar & Price, 1996;Yang et al, 1996). For the expression of some genes, the involvement of s B is essential, whereas for others it seems to be only involved because it can be replaced by alternative stress-induction mechanisms .…”

Section: Sigma B-controlled Genesmentioning

confidence: 99%

Proteome analysis in the study of the bacterial heat‐shock response

Rosen

Ron

2002

Mass Spectrometry Reviews

129

112

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In recent years, it has become clear that, in addition to the regulation of the expression of specific genes, there are global regulatory systems that control the simultaneous expression of a large number of genes in response to a variety of environmental stresses. The first of these global control systems, and of substantial importance, is the heat-shock response. The heat-shock response is characterized by the induction of a large set of proteins (heat-shock proteins-HSPs) upon shifts to higher temperature and upon exposure to conditions in which proteins are denatured (i.e., alcohols, heavy metals). The heat-shock response is universal and many of the heat-shock proteins are highly conserved among species. In bacteria, the heat-shock response has been studied extensively in several Gram-positive bacteria (Bacillus subtilis) and in the Gram-negative bacteria (i.e., Escherichia coli, Agrobacterium tumefaciens). The first recognition of the molecular abundance of the bacterial heat-shock proteins took place with the introduction of high-resolution two-dimensional polyacrylamide gels (2D gels) to analyze complex mixtures of cellular proteins. Two-dimensional gels, followed by mass spectrometry, were used to define the heat-shock stimulons in several bacteria, and to study the regulatory elements that control the heat-shock response. Here, we review the heat-shock response and its regulation in bacteria. The review will emphasize the use of proteome analysis in the study of this response, and will point out those open questions that can be investigated with proteomics, including mass spectrometry techniques.

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“…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.…”

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confidence: 99%

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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Isolation and characterization of csbB, a gene controlled by Bacillus subtilis general stress transcription factor σB

Cited by 26 publications

References 23 publications

Modification of Streptococcus mutans Cnm by PgfS Contributes to Adhesion, Endothelial Cell Invasion, and Virulence

Modification of Streptococcus mutans Cnm by PgfS Contributes to Adhesion, Endothelial Cell Invasion, and Virulence

Proteome analysis in the study of the bacterial heat‐shock response

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

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Isolation and characterization of csbB, a gene controlled by Bacillus subtilis general stress transcription factor σB

Cited by 26 publications

References 23 publications

Modification of Streptococcus mutans Cnm by PgfS Contributes to Adhesion, Endothelial Cell Invasion, and Virulence

Modification of Streptococcus mutans Cnm by PgfS Contributes to Adhesion, Endothelial Cell Invasion, and Virulence

Proteome analysis in the study of the bacterial heat‐shock response

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

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