Analysis of σ54-dependent genes in Enterococcus faecalis: a mannose PTS permease (EIIMan) is involved in sensitivity to a bacteriocin, mesentericin Y105

Héchard, Yann; Pelletier, Christelle; Cenatiempo, Y.; Frère, Jacques

doi:10.1099/00221287-147-6-1575

Cited by 122 publications

(111 citation statements)

References 27 publications

Supporting

Mentioning

106

Contrasting

Unclassified

Order By: Relevance

“…In addition, the EIID domain of the Mpt PTS possesses a C-terminal extension characteristic of mannose/glucose-specific PTS, and the various sugar-specific EII Mpt components exhibit the strongest similarity to those of the recently characterized mannose/glucose PTS of L. casei (975). Homologs of the Mpt PTS are present in E. faecalis and Listeria innocua, and the absence of expression of the mpt operon in these organisms also leads to resistance towards class IIa bacteriocins such as mesentericin Y105 for E. faecalis (320) and pediocin AcH for L. innocua (959). The expression of the mpt operon containing the mptA, mptC, and mptD genes, which encode EIIAB, EIIC, and EIID, respectively, depends on 54 (RpoN) and on a LevR-like protein, which was called ManR.…”

Section: Discussionmentioning

confidence: 99%

How Phosphotransferase System-Related Protein Phosphorylation Regulates Carbohydrate Metabolism in Bacteria

Deutscher

Francke

Postma

2006

Microbiol Mol Biol Rev

1,191

769

View full text Add to dashboard Cite

SUMMARY The phosphoenolpyruvate(PEP):carbohydrate phosphotransferase system (PTS) is found only in bacteria, where it catalyzes the transport and phosphorylation of numerous monosaccharides, disaccharides, amino sugars, polyols, and other sugar derivatives. To carry out its catalytic function in sugar transport and phosphorylation, the PTS uses PEP as an energy source and phosphoryl donor. The phosphoryl group of PEP is usually transferred via four distinct proteins (domains) to the transported sugar bound to the respective membrane component(s) (EIIC and EIID) of the PTS. The organization of the PTS as a four-step phosphoryl transfer system, in which all P derivatives exhibit similar energy (phosphorylation occurs at histidyl or cysteyl residues), is surprising, as a single protein (or domain) coupling energy transfer and sugar phosphorylation would be sufficient for PTS function. A possible explanation for the complexity of the PTS was provided by the discovery that the PTS also carries out numerous regulatory functions. Depending on their phosphorylation state, the four proteins (domains) forming the PTS phosphorylation cascade (EI, HPr, EIIA, and EIIB) can phosphorylate or interact with numerous non-PTS proteins and thereby regulate their activity. In addition, in certain bacteria, one of the PTS components (HPr) is phosphorylated by ATP at a seryl residue, which increases the complexity of PTS-mediated regulation. In this review, we try to summarize the known protein phosphorylation-related regulatory functions of the PTS. As we shall see, the PTS regulation network not only controls carbohydrate uptake and metabolism but also interferes with the utilization of nitrogen and phosphorus and the virulence of certain pathogens.

show abstract

Section: Discussionmentioning

confidence: 99%

How Phosphotransferase System-Related Protein Phosphorylation Regulates Carbohydrate Metabolism in Bacteria

Deutscher

Francke

Postma

2006

Microbiol Mol Biol Rev

1,191

769

View full text Add to dashboard Cite

show abstract

“…ORFs coding for SigH and SigV are not expressed in S and R growth conditions (Supplemental Table SD; the ppRNome browser), hence we did not expect to find TSSs whose promoter regions would carry consensus sequences recognized by either one of these factors. In contrast, the sigN encoding sequence is transcribed and we sought manually for the consensus sequence of SigN-dependent promoter ahead of TSSs mapped (−24/−12; TTGCCACNNNNNTTGCT) (Buck et al 2000;Héchard et al 2001;Iyer and Hancock 2012). Only six corresponding locations were found across the whole genome: upstream ORFs coding for components of phosphor-sugar transfer systems (PTS), ef0019, ef1012, ef1017, ef1954, ef3210, and fabF-2 coding for an enzyme involved in fatty acid and biotin metabolism.…”

Section: Motif Detection and Promoter Features In The E Faecalis Genomementioning

confidence: 99%

Whole-genome mapping of 5′ RNA ends in bacteria by tagged sequencing: a comprehensive view in Enterococcus faecalis

Innocenti

Golumbeanu

d’Hérouël

et al. 2015

RNA

View full text Add to dashboard Cite

Enterococcus faecalis is the third cause of nosocomial infections. To obtain the first snapshot of transcriptional organizations in this bacterium, we used a modified RNA-seq approach enabling to discriminate primary from processed 5 ′ RNA ends. We also validated our approach by confirming known features in Escherichia coli. We mapped 559 transcription start sites (TSSs) and 352 processing sites (PSSs) in E. faecalis. A blind motif search retrieved canonical features of SigA-and SigN-dependent promoters preceding transcription start sites mapped. We discovered 85 novel putative regulatory RNAs, small-and antisense RNAs, and 72 transcriptional antisense organizations. Presented data constitute a significant insight into bacterial RNA landscapes and a step toward the inference of regulatory processes at transcriptional and post-transcriptional levels in a comprehensive manner.

show abstract

“…Recently, a number of reports have indicated that pediocinlike bacteriocins exploit the mannose PTS sugar permease as a receptor when attacking Listeria and Enterococcus species (Hechard et al, 2001;Gravesen et al, 2002), and that many spontaneous mutants of Listeria resistant to this group of bacteriocins were found to exhibit a reduced synthesis of one of the subunits of the permease complex (Gravesen et al, 2002). Spontaneous mutants of the indicator strain E. faecium P13 resistant to penocin A or pediocin PA-1 were found to occur at high frequencies and also displayed cross-resistance towards each other (data not shown).…”

Section: Cross-resistance Between Penocin a And The Other Pediocin-limentioning

confidence: 99%

Data mining and characterization of a novel pediocin-like bacteriocin system from the genome of Pediococcus pentosaceus ATCC 25745

et al. 2006

View full text Add to dashboard Cite

The genome of Pediococcus pentosaceus ATCC 25745 contains a gene cluster that resembles a regulated bacteriocin system. The gene cluster has an operon-like structure consisting of a putative pediocin-like bacteriocin gene (termed penA) and a potential immunity gene (termed peiA). Genetic determinants involved in bacteriocin transport and regulation are also found in proximity to penA and peiA but the so-called accessory gene involved in transport and the inducer gene involved in regulation are missing. Consequently, this bacterium is a poor bacteriocin producer. To analyse the potency of the putative bacteriocin operon, the two genes penA-peiA were heterologously expressed in a Lactobacillus sakei host that contains the complete apparatus for gene activation, maturation and externalization of bacteriocins. It was demonstrated that the heterologous host expressing penA and peiA produced a strong bacteriocin activity; in addition, the host became immune to its own bacteriocin, identifying the gene pair penA-peiA as a potent bacteriocin system. The novel pediocin-like bacteriocin, termed penocin A, has an isotopic mass [M+H] + of 4684?6 Da as determined by mass spectrometry; this value corresponds well to the expected size of the mature 42 aa peptide containing a disulfide bridge. The bacteriocin is heat-stable but protease-sensitive and has a calculated pI of 9?45. Penocin A has a relatively broad inhibition spectrum, including pathogenic Listeria and Clostridium species. Immediately upstream of the regulatory genes reside some features that resemble remnants of a disrupted inducer gene. This degenerate gene was restored and shown to encode a double-glycine leader-containing peptide. Furthermore, expression of the restored gene triggered high bacteriocin production in P. pentosaceus ATCC 25745, thus confirming its role as an inducer in the pen regulon.

show abstract

Analysis of σ54-dependent genes in Enterococcus faecalis: a mannose PTS permease (EIIMan) is involved in sensitivity to a bacteriocin, mesentericin Y105

Cited by 122 publications

References 27 publications

How Phosphotransferase System-Related Protein Phosphorylation Regulates Carbohydrate Metabolism in Bacteria

How Phosphotransferase System-Related Protein Phosphorylation Regulates Carbohydrate Metabolism in Bacteria

Whole-genome mapping of 5′ RNA ends in bacteria by tagged sequencing: a comprehensive view in Enterococcus faecalis

Data mining and characterization of a novel pediocin-like bacteriocin system from the genome of Pediococcus pentosaceus ATCC 25745

Contact Info

Product

Resources

About