Novel listerial genetic loci conferring enhanced barotolerance in Escherichia coli

Considine, Kiera; Sleator, Roy D.; Kelly, Alan L.; Fitzgerald, Gerald F.; Hill, Colin

doi:10.1111/j.1365-2672.2010.04924.x

Cited by 10 publications

(7 citation statements)

References 45 publications

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“…Microscopy was performed essentially as described by Considine et al 48 Safranin (0.25%) stained samples of individual strains were viewed using Bright-field light microscopy at 1000 × magnification to determine cell morphology. For scanning electron microscopy (SEM), overnight cultures in TSB ± 7% added NaCl (5 mL in a 30 mL round-bottomed tube) were centrifuged at 5,000 rpm × 10 min.…”

Section: Methodsmentioning

confidence: 99%

A single point mutation in the listerialbetLσ^A-dependent promoter leads to improved osmo- and chill-tolerance and a morphological shift at elevated osmolarity

et al. 2013

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Betaine uptake in Listeria monocytogenes is mediated by three independent transport systems, the simplest of which in genetic terms is the secondary transporter BetL. Using a random mutagenesis approach, based on the E. coli XL1 Red mutator strain, we identified a single point mutation in a putative promoter region upstream of the BetL coding region which leads to a significant increase in betL transcript levels under osmo- and chill-stress conditions and a concomitant increase in stress tolerance. Furthermore, the mutation appears to counter the heretofore unreported “twisted” cell morphology observed for L. monocytogenes grown at elevated osmolarities in tryptone soy broth.

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Section: Methodsmentioning

confidence: 99%

A single point mutation in the listerialbetLσ^A-dependent promoter leads to improved osmo- and chill-tolerance and a morphological shift at elevated osmolarity

et al. 2013

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“…The study, which represents the first use of agar plates as a novel methodology for screening genome libraries using HPP, identified systems involved in quorum sensing (Agr), flagellar machinery (Mot) and cytokinesis (EzrA) as conferring enhanced pressure resistance when expressed against an E. coli background. 43 In a follow-on study, 44 failure to disrupt EzrA (encoded by lmo1594) revealed that the protein is essential for the growth of L. monocytoenes. Thus, while gene deletion proved impossible; over-expression of lmo1594 confirmed a role for the protein in listerial barotolerance, resulting in significantly improved survival rates at 300 MPa.…”

Section: Bile Tolerancementioning

confidence: 99%

Under the microscope: From pathogens to probiotics and back

Sleator¹

2015

Bioengineered

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“…S. aureus EzrA plays a role in the localization of GpsB and PBP1, as it does in B. subtilis [12], [13]. EzrA has been reported to be essential in the rod shaped bacterium, Listeria monocytogenes , although its role in cell division and cell wall synthesis has not been well characterized in this organism [14].…”

Section: Introductionmentioning

confidence: 99%

Functional Domain Analysis of the Cell Division Inhibitor EzrA

2014

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The precise spatial and temporal control of bacterial cell division is achieved through the balanced actions of factors that inhibit assembly of the tubulin-like protein FtsZ at aberrant subcellular locations or promote its assembly at the future sites of division. In Bacillus subtilis, the membrane anchored cell division protein EzrA, interacts directly with FtsZ to prevent aberrant FtsZ assembly at cell poles and contributes to the inherently dynamic nature of the cytokinetic ring. Recent work suggests EzrA also serves as a scaffolding protein to coordinate lateral growth with cell wall biosynthesis through interactions with a host of proteins, a finding consistent with EzrA's four extensive coiled-coil domains. In a previous study we identified a conserved patch of residues near EzrA's C-terminus (the QNR motif) that are critical for maintenance of a dynamic cytokinetic ring, but dispensable for EzrA-mediated inhibition of FtsZ assembly at cell poles. In an extension of this work, here we report that EzrA's two C-terminal coiled-coils function in concert with the QNR motif to mediate interactions with FtsZ and maintain the dynamic nature of the cytokinetic ring. In contrast, EzrA's two N-terminal coiled-coils are dispensable for interaction between EzrA and FtsZ in vitro and in vivo, but required for EzrA mediated inhibition of FtsZ assembly at cell poles. Finally, chimeric analysis indicates that EzrA's transmembrane anchor plays a generic role: concentrating EzrA at the plasma membrane where presumably it can most effectively modulate FtsZ assembly.

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Novel listerial genetic loci conferring enhanced barotolerance in Escherichia coli

Cited by 10 publications

References 45 publications

A single point mutation in the listerialbetLσ^A-dependent promoter leads to improved osmo- and chill-tolerance and a morphological shift at elevated osmolarity

A single point mutation in the listerialbetLσ^A-dependent promoter leads to improved osmo- and chill-tolerance and a morphological shift at elevated osmolarity

Under the microscope: From pathogens to probiotics and back

Functional Domain Analysis of the Cell Division Inhibitor EzrA

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Novel listerial genetic loci conferring enhanced barotolerance in Escherichia coli

Cited by 10 publications

References 45 publications

A single point mutation in the listerialbetLσA-dependent promoter leads to improved osmo- and chill-tolerance and a morphological shift at elevated osmolarity

A single point mutation in the listerialbetLσA-dependent promoter leads to improved osmo- and chill-tolerance and a morphological shift at elevated osmolarity

Under the microscope: From pathogens to probiotics and back

Functional Domain Analysis of the Cell Division Inhibitor EzrA

Contact Info

Product

Resources

About

A single point mutation in the listerialbetLσ^A-dependent promoter leads to improved osmo- and chill-tolerance and a morphological shift at elevated osmolarity

A single point mutation in the listerialbetLσ^A-dependent promoter leads to improved osmo- and chill-tolerance and a morphological shift at elevated osmolarity