Functional independence of a variant LuxOPL91 from a non-O1 non-O139 Vibrio cholerae over the activity of CsrA and Fis

Dongre, Mitesh; Tripathi, Ratnakar; Jain, Vibhu; Raychaudhuri, Saumya

doi:10.1099/jmm.0.47606-0

Cited by 3 publications

(2 citation statements)

References 18 publications

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“…The other variant was designated LuxO PL91 and harbours a natural deletion of 12 amino acids (I 80 DTAVEAMRHGA 91 ) in the N-terminal region (Raychaudhuri et al, 2006). Additionally, LuxO PL91 does not require any input from LuxU, CsrA and Fis, a property akin to LuxO D47E, and maintains its activity even at high cell density, thus exerting a profound influence on the physiology of V. cholerae strain PL91 (Raychaudhuri et al, 2006;Dongre et al, 2008).…”

Section: Jmm Correspondencementioning

confidence: 99%

“…Correspondence to elucidate the functional status of LuxO (Vance et al, 2003;Raychaudhuri et al, 2006), the high cell density cell-free supernatants of all recombinant strains of MM307 and SC134 were harvested and examined for protease production using an azocasein assay as described elsewhere (Dongre et al, 2008). We observed an inhibition of protease production in MM307 and SC134 strains harbouring alanine congeners of two residues, namely histidine (H89A) and glycine (G90A), at high cell density, while MM307 and SC134 strains carrying alanine derivatives of I 80 , D 81 , T 82 , V 84 , E 85 , M 87 , R 88 and pNL (control plasmid for alanine at positions A 83 , A 86 and A 91 ) showed protease production under similar conditions (Fig.…”

Section: Primer Name Sequence (5 §A3 §)mentioning

confidence: 99%

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Alanine-scanning mutagenesis of selected residues in the N-terminal region alters the functionality of LuxO: lessons from a natural variant LuxOPL91

Dongre

Khatri

Dureja

et al. 2011

Journal of Medical Microbiology

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Section: Jmm Correspondencementioning

confidence: 99%

Section: Primer Name Sequence (5 §A3 §)mentioning

confidence: 99%

Alanine-scanning mutagenesis of selected residues in the N-terminal region alters the functionality of LuxO: lessons from a natural variant LuxOPL91

Dongre

Khatri

Dureja

et al. 2011

Journal of Medical Microbiology

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Campylobacter jejuni CsrA complements an Escherichia coli csrA mutation for the regulation of biofilm formation, motility and cellular morphology but not glycogen accumulation

Fields

Thompson

2012

BMC Microbiology

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BackgroundAlthough Campylobacter jejuni is consistently ranked as one of the leading causes of bacterial diarrhea worldwide, the mechanisms by which C. jejuni causes disease and how they are regulated have yet to be clearly defined. The global regulator, CsrA, has been well characterized in several bacterial genera and is known to regulate a number of independent pathways via a post transcriptional mechanism, but remains relatively uncharacterized in the genus Campylobacter. Previously, we reported data illustrating the requirement for CsrA in several virulence related phenotypes of C. jejuni strain 81–176, indicating that the Csr pathway is important for Campylobacter pathogenesis.ResultsWe compared the Escherichia coli and C. jejuni orthologs of CsrA and characterized the ability of the C. jejuni CsrA protein to functionally complement an E. coli csrA mutant. Phylogenetic comparison of E. coli CsrA to orthologs from several pathogenic bacteria demonstrated variability in C. jejuni CsrA relative to the known RNA binding domains of E. coli CsrA and in several amino acids reported to be involved in E. coli CsrA-mediated gene regulation. When expressed in an E. coli csrA mutant, C. jejuni CsrA succeeded in recovering defects in motility, biofilm formation, and cellular morphology; however, it failed to return excess glycogen accumulation to wild type levels.ConclusionsThese findings suggest that C. jejuni CsrA is capable of efficiently binding some E. coli CsrA binding sites, but not others, and provide insight into the biochemistry of C. jejuni CsrA.

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Identification of critical amino acids in the DNA binding domain of LuxO: Lessons from a constitutive active LuxO

Surin,

Singh,

Kaur

et al. 2024

PLoS ONE

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Quorum sensing plays a vital role in the environmental and host life cycles of Vibrio cholerae. The quorum-sensing circuit involves the consorted action of autoinducers, small RNAs, and regulatory proteins to control a plethora of physiological events in this bacterium. Among the regulatory proteins, LuxO is considered a low-cell-density master regulator. It is a homolog of NtrC, a two-component response regulator. NtrC belongs to an evolving protein family that works with the alternative sigma factor σ54 to trigger gene transcription. Structurally, these proteins comprise 3 domains: a receiver domain, a central AAA+ATPase domain, and a C-terminal DNA-binding domain (DBD). LuxO communicates with its cognate promoters by employing its DNA binding domain. In the present study, we desired to identify the critical residues in the DBD of LuxO. Our combined mutagenesis and biochemical assays resulted in the identification of eleven residues that contribute significantly to LuxO regulatory function.

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Functional independence of a variant LuxOPL91 from a non-O1 non-O139 Vibrio cholerae over the activity of CsrA and Fis

Cited by 3 publications

References 18 publications

Alanine-scanning mutagenesis of selected residues in the N-terminal region alters the functionality of LuxO: lessons from a natural variant LuxOPL91

Alanine-scanning mutagenesis of selected residues in the N-terminal region alters the functionality of LuxO: lessons from a natural variant LuxOPL91

Campylobacter jejuni CsrA complements an Escherichia coli csrA mutation for the regulation of biofilm formation, motility and cellular morphology but not glycogen accumulation

Identification of critical amino acids in the DNA binding domain of LuxO: Lessons from a constitutive active LuxO

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