Supportive and inhibitory elements of a putative PrfA‐dependent promoter in<i>Listeria monocytogenes</i>

Luo, Qiong; Herler, Michael; Müller-Altrock, Stefanie; Goebel, Werner

doi:10.1111/j.1365-2958.2005.04417.x

Cited by 5 publications

(2 citation statements)

References 50 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…A PrfAdependent promoter consists of a 210 box recognized by the sigma factor A (SigA). A 235 box is not required, but a distance of 21 or 22 bp between the 210 box and the PrfA box has been shown to be crucial for efficient transcription of the regulated genes Luo et al, 2004Luo et al, , 2005.…”

Section: Introductionmentioning

confidence: 99%

Modulation of PrfA activity in Listeria monocytogenes upon growth in different culture media

et al. 2008

Self Cite

View full text Add to dashboard Cite

PrfA is the major transcriptional activator of most virulence genes of Listeria monocytogenes. Its activity is modulated by a variety of culture conditions. Here, we studied the PrfA activity in the L. monocytogenes wild-type strain EGD and an isogenic prfA deletion mutant (EGDDprfA) carrying multiple copies of the wild-type prfA or the mutant prfA* gene (strains EGDDprfApPrfA and EGDDprfApPrfA*) in response to growth in brain heart infusion (BHI), Luria-Bertani broth (LB) or a defined minimal medium (MM) supplemented with one of the three phosphotransferase system (PTS) carbohydrates, glucose, mannose and cellobiose, or the non-PTS carbon source glycerol. Low PrfA activity was observed in the wild-type strain in BHI and LB with all of these carbon sources, while PrfA activity was high in minimal medium in the presence of glycerol. EGDDprfApPrfA*, expressing a large amount of PrfA* protein, showed high PrfA activity under all growth conditions. In contrast, strain EGDDprfApPrfA, expressing an equally high amount of PrfA protein, showed high PrfA activity only when cultured in BHI, and not in LB or MM (in the presence of any of the carbon sources). A ptsH mutant (lacking a functional HPr) was able to grow in BHI but not in LB or MM, regardless of which of the four carbon sources was added, suggesting that in LB and MM the uptake of the used PTS carbohydrates and the catabolism of glycerol are fully dependent on the functional common PTS pathway. The BHI culture medium, in contrast, apparently contains carbon sources (supporting listerial growth) which are taken up and metabolized by L. monocytogenes independently of the common PTS pathway. The growth rates of L. monocytogenes were strongly reduced in the presence of large amounts of PrfA (or PrfA*) protein when growing in MM, but were less reduced in LB and only slightly reduced in BHI. The expression of the genes encoding the PTS permeases of L. monocytogenes was determined in the listerial strains under the applied growth conditions. The data obtained further support the hypothesis that PrfA activity correlates with the expression level and the phosphorylation state of specific PTS permeases.

show abstract

Section: Introductionmentioning

confidence: 99%

Modulation of PrfA activity in Listeria monocytogenes upon growth in different culture media

et al. 2008

Self Cite

View full text Add to dashboard Cite

show abstract

“…A typical Ϫ35 box is normally not found, and its presence may even inhibit the activation by PrfA. Certain sequences within the interspace region (between the Ϫ10 and the PrfA boxes) or adjacent to these sequences may positively or negatively influence the functionality of a PrfA-dependent promoter (15,30,31).…”

mentioning

confidence: 99%

Species-Specific Differences in the Activity of PrfA,the Key Regulator of Listerial VirulenceGenes

et al. 2006

Self Cite

View full text Add to dashboard Cite

PrfA, the master regulator of LIPI-1, is indispensable for the pathogenesis of the human pathogen Listeria monocytogenes and the animal pathogen Listeria ivanovii. PrfA is also present in the apathogenic species Listeria seeligeri, and in this study, we elucidate the differences between PrfA proteins from the pathogenic and apathogenic species of the genus Listeria. PrfA proteins of L. monocytogenes (PrfA Lm and PrfA* Lm ), L. ivanovii (PrfA Li ), and L. seeligeri (PrfA Ls ) were purified, and their equilibrium constants for binding to the PrfA box of the hly promoter (Phly Lm ) were determined by surface plasmon resonance. In addition, the capacities of these PrfA proteins to bind to the PrfA-dependent promoters Phly and PactA and to form ternary complexes together with RNA polymerase were analyzed in electrophoretic mobility shift assays, and their abilities to initiate transcription in vitro starting at these promoters were compared. The results show

show abstract

The PrfA virulence regulon

Scortti

Monzó

Lacharme-Lora

et al. 2007

Microbes and Infection

204

229

View full text Add to dashboard Cite

Supportive and inhibitory elements of a putative PrfA‐dependent promoter inListeria monocytogenes

Cited by 5 publications

References 50 publications

Modulation of PrfA activity in Listeria monocytogenes upon growth in different culture media

Modulation of PrfA activity in Listeria monocytogenes upon growth in different culture media

Species-Specific Differences in the Activity of PrfA,the Key Regulator of Listerial VirulenceGenes

The PrfA virulence regulon

Contact Info

Product

Resources

About