scholarly journals A Novel Role for Enzyme I of the Vibrio cholerae Phosphoenolpyruvate Phosphotransferase System in Regulation of Growth in a Biofilm

2007 ◽  
Vol 190 (1) ◽  
pp. 311-320 ◽  
Author(s):  
Laetitia Houot ◽  
Paula I. Watnick
Keyword(s):  
Vibrio Cholerae ◽  
Sugar Transport ◽  
Phosphotransferase System ◽  
Potent Inducer ◽  
Inducer Exclusion ◽  
Genes Encoding ◽  
Cell Components ◽  
Specific Regulation ◽  
Enzyme I

ABSTRACT Glucose is a universal energy source and a potent inducer of surface colonization for many microbial species. Highly efficient sugar assimilation pathways ensure successful competition for this preferred carbon source. One such pathway is the phosphoenolpyruvate phosphotransferase system (PTS), a multicomponent sugar transport system that phosphorylates the sugar as it enters the cell. Components required for transport of glucose through the PTS include enzyme I, histidine protein, enzyme IIAGlc, and enzyme IIBCGlc. In Escherichia coli, components of the PTS fulfill many regulatory roles, including regulation of nutrient scavenging and catabolism, chemotaxis, glycogen utilization, catabolite repression, and inducer exclusion. We previously observed that genes encoding the components of the Vibrio cholerae PTS were coregulated with the vps genes, which are required for synthesis of the biofilm matrix exopolysaccharide. In this work, we identify the PTS components required for transport of glucose and investigate the role of each of these components in regulation of biofilm formation. Our results establish a novel role for the phosphorylated form of enzyme I in specific regulation of biofilm-associated growth. As the PTS is highly conserved among bacteria, the enzyme I regulatory pathway may be relevant to a number of biofilm-based infections.

scholarly journals Cloning and Expression of the Listeria monocytogenes Scott A ptsH and ptsI Genes, Coding for HPr and Enzyme I, Respectively, of the Phosphotransferase System

1998 ◽  
Vol 64 (9) ◽  
pp. 3147-3152 ◽  
Author(s):  
Douglas P. Christensen ◽  
Andrew K. Benson ◽  
Robert W. Hutkins
Keyword(s):  
Listeria Monocytogenes ◽  
High Energy ◽  
Transcription Unit ◽  
Cloning And Expression ◽  
Nucleotide Sequence Analysis ◽  
Phosphotransferase System ◽  
Genes Encoding ◽  
And Control ◽  
Enzyme I

ABSTRACT The phosphoenolpyruvate (PEP)-dependent phosphotransferase system (PTS) utilizes high-energy phosphate present in PEP to drive the uptake of several different carbohydrates in bacteria. In order to examine the role of the PTS in the physiology of Listeria monocytogenes, we identified the ptsH andptsI genes encoding the HPr and enzyme I proteins, respectively, of the PTS. Nucleotide sequence analysis indicated that the predicted proteins are nearly 70% similar to HPr and enzyme I proteins from other organisms. Purified L. monocytogenesHPr overexpressed in Escherichia coli was also capable of complementing an HPr defect in heterologous extracts ofStaphylococcus aureus ptsH mutants. Additional studies of the transcriptional organization and control indicated that theptsH and ptsI genes are organized into a transcription unit that is under the control of a consensus-like promoter and that expression of these genes is mediated by glucose availability and pH or by by-products of glucose metabolism.

PTS-Mediated Regulation of the Transcription Activator MtlR from Different Species: Surprising Differences despite Strong Sequence Conservation

2015 ◽  
Vol 25 (2-3) ◽  
pp. 94-105 ◽  
Author(s):  
Philippe Joyet ◽  
Meriem Derkaoui ◽  
Houda Bouraoui ◽  
Josef Deutscher
Keyword(s):  
Bacillus Subtilis ◽  
Lactobacillus Casei ◽  
Sequence Conservation ◽  
Geobacillus Stearothermophilus ◽  
Transcription Activator ◽  
Phosphotransferase System ◽  
Transcription Regulator ◽  
Regulatory Domains ◽  
Genes Encoding ◽  
Enzyme I

The hexitol <smlcap>D</smlcap>-mannitol is transported by many bacteria via a phosphoenolpyruvate (PEP):carbohydrate phosphotransferase system (PTS). In most Firmicutes, the transcription activator MtlR controls the expression of the genes encoding the <smlcap>D</smlcap>-mannitol-specific PTS components and <smlcap>D</smlcap>-mannitol-1-P dehydrogenase. MtlR contains an N-terminal helix-turn-helix motif followed by an Mga-like domain, two PTS regulation domains (PRDs), an EIIB<sup>Gat</sup>- and an EIIA<sup>Mtl</sup>-like domain. The four regulatory domains are the target of phosphorylation by PTS components. Despite strong sequence conservation, the mechanisms controlling the activity of MtlR from <i>Lactobacillus casei</i>, <i>Bacillus subtilis</i> and <i>Geobacillus stearothermophilus</i> are quite different. Owing to the presence of a tyrosine in place of the second conserved histidine (His) in PRD2, <i>L. casei</i> MtlR is not phosphorylated by Enzyme I (EI) and HPr. When the corresponding His in PRD2 of MtlR from <i>B. subtilis</i> and <i>G. stearothermophilus</i> was replaced with alanine, the transcription regulator was no longer phosphorylated and remained inactive. Surprisingly, <i>L. casei</i> MtlR functions without phosphorylation in PRD2 because in a <i>ptsI</i> (EI) mutant MtlR is constitutively active. EI inactivation prevents not only phosphorylation of HPr, but also of the PTS<sup>Mtl</sup> components, which inactivate MtlR by phosphorylating its EIIB<sup>Gat</sup>- or EIIA<sup>Mtl</sup>-like domain. This explains the constitutive phenotype of the <i>ptsI</i> mutant. The absence of EIIB<sup>Mtl</sup>-mediated phosphorylation leads to induction of the <i>L. casei</i><i>mtl </i>operon. This mechanism resembles <i>mtlARFD</i> induction in <i>G. stearothermophilus</i>, but differs from EIIA<sup>Mtl</sup>-mediated induction in <i>B. subtilis</i>. In contrast to <i>B. subtilis</i> MtlR, <i>L. casei</i> MtlR activation does not require sequestration to the membrane via the unphosphorylated EIIB<sup>Mtl</sup> domain.

scholarly journals Genetic evidence for the role of a bacterial phosphotransferase system in sugar transport.

1967 ◽  
Vol 58 (5) ◽  
pp. 1963-1970 ◽  
Author(s):  
R. D. Simoni ◽  
M. Levinthal ◽  
F. D. Kundig ◽  
W. Kundig ◽  
B. Anderson ◽  
...  
Keyword(s):  
Sugar Transport ◽  
Genetic Evidence ◽  
Phosphotransferase System ◽  
Bacterial Phosphotransferase System

scholarly journals Activation of the Vibrio cholerae SOS Response Is Not Required for Intestinal Cholera Toxin Production or Colonization

2006 ◽  
Vol 74 (2) ◽  
pp. 927-930 ◽  
Author(s):  
Mariam Quinones ◽  
Brigid M. Davis ◽  
Matthew K. Waldor
Keyword(s):  
Cholera Toxin ◽  
Vibrio Cholerae ◽  
Sos Response ◽  
Toxin Production ◽  
Mrna Levels ◽  
Suckling Mouse ◽  
Potent Inducer ◽  
Genes Encoding ◽  
Mouse Intestine ◽  
Ctx Prophage

ABSTRACT Cholera toxin, one of the main virulence factors of Vibrio cholerae, is encoded in the genome of CTXφ, a V. cholerae-specific lysogenic filamentous bacteriophage. Although the genes encoding cholera toxin, ctxAB, are known to have their own promoter, the toxin genes can also be transcribed from an upstream CTXφ promoter, PrstA . The V. cholerae SOS response to DNA damage induces the CTX prophage by stimulating gene expression initiating from PrstA . Here, we investigated whether ctxA mRNA levels increase along with the levels of the transcripts for the other CTXφ genes following stimulation of the V. cholerae SOS response. Treatment of V. cholerae with the SOS-inducing agent mitomycin C increased the level of ctxA mRNA approximately sevenfold, apparently by augmenting the activity of PrstA . However, using suckling mice as a model host, we found that intraintestinal ctxA transcription does not depend on PrstA . In fact, the suckling mouse intestine does not appear to be a potent inducer of the V. cholerae SOS response. Furthermore, alleviation of LexA-mediated repression of the V. cholerae SOS regulon was not required for V. cholerae growth in the suckling mouse intestine. Our observations suggest that pathogenicity of V. cholerae does not depend on its SOS response.

scholarly journals Iron and Fur Regulation in Vibrio cholerae and the Role of Fur in Virulence

2005 ◽  
Vol 73 (12) ◽  
pp. 8167-8178 ◽  
Author(s):  
Alexandra R. Mey ◽  
Elizabeth E. Wyckoff ◽  
Vanamala Kanukurthy ◽  
Carolyn R. Fisher ◽  
Shelley M. Payne
Keyword(s):  
Gene Expression ◽  
Vibrio Cholerae ◽  
Iron Acquisition ◽  
Bacterial Species ◽  
Regulation Of Gene Expression ◽  
Transport Systems ◽  
Infant Mouse ◽  
Genes Encoding ◽  
Regulatory Functions

ABSTRACT Regulation of iron uptake and utilization is critical for bacterial growth and for prevention of iron toxicity. In many bacterial species, this regulation depends on the iron-responsive master regulator Fur. In this study we report the effects of iron and Fur on gene expression in Vibrio cholerae. We show that Fur has both positive and negative regulatory functions, and we demonstrate Fur-independent regulation of gene expression by iron. Nearly all of the known iron acquisition genes were repressed by Fur under iron-replete conditions. In addition, genes for two newly identified iron transport systems, Feo and Fbp, were found to be negatively regulated by iron and Fur. Other genes identified in this study as being induced in low iron and in the fur mutant include those encoding superoxide dismutase (sodA), fumarate dehydratase (fumC), bacterioferritin (bfr), bacterioferritin-associated ferredoxin (bfd), and multiple genes of unknown function. Several genes encoding iron-containing proteins were repressed in low iron and in the fur mutant, possibly reflecting the need to reserve available iron for the most critical functions. Also repressed in the fur mutant, but independently of iron, were genes located in the V. cholerae pathogenicity island, encoding the toxin-coregulated pilus (TCP), and genes within the V. cholerae mega-integron. The fur mutant exhibited very weak autoagglutination, indicating a possible defect in expression or assembly of the TCP, a major virulence factor of V. cholerae. Consistent with this observation, the fur mutant competed poorly with its wild-type parental strain for colonization of the infant mouse gut.

scholarly journals Distribution and Functions of Phosphotransferase System Genes in the Genome of the Lactic Acid Bacterium Oenococcus oeni

2013 ◽  
Vol 79 (11) ◽  
pp. 3371-3379 ◽  
Author(s):  
Zohra Jamal ◽  
Cécile Miot-Sertier ◽  
François Thibau ◽  
Lucie Dutilh ◽  
Aline Lonvaud-Funel ◽  
...  
Keyword(s):  
Lactic Acid ◽  
Lactic Acid Bacterium ◽  
Oenococcus Oeni ◽  
Phosphotransferase System ◽  
Content Type ◽  
Low Concentrations ◽  
Perfect Adaptation ◽  
Form Part ◽  
Genes Encoding ◽  
Enzyme I

ABSTRACTOenococcus oeni, the lactic acid bacterium primarily responsible for malolactic fermentation in wine, is able to grow on a large variety of carbohydrates, but the pathways by which substrates are transported and phosphorylated in this species have been poorly studied. We show that the genes encoding the general phosphotransferase proteins, enzyme I (EI) and histidine protein (HPr), as well as 21 permease genes (3 isolated ones and 18 clustered into 6 distinct loci), are highly conserved among the strains studied and may form part of theO. oenicore genome. Additional permease genes differentiate the strains and may have been acquired or lost by horizontal gene transfer events. The coreptsgenes are expressed, and permease gene expression is modulated by the nature of the bacterial growth substrate. DecryptifiedO. oenicells are able to phosphorylate glucose, cellobiose, trehalose, and mannose at the expense of phosphoenolpyruvate. These substrates are present at low concentrations in wine at the end of alcoholic fermentation. The phosphotransferase system (PTS) may contribute to the perfect adaptation ofO. oenito its singular ecological niche.

Sign in / Sign up

Export Citation Format

Share Document