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The HtrA chaperone monitors sortase-assembled pilus biogenesis in E. faecalis

ABSTRACT: The HtrA chaperone monitors sortase-assembled pilus biogenesis in E. faecalis

PROVIDER: PRJNA1087743 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR28343251_1.fastq.gz	Fastqsanger.gz
	SRR28343251_2.fastq.gz	Fastqsanger.gz
	SRR28343252_1.fastq.gz	Fastqsanger.gz
	SRR28343252_2.fastq.gz	Fastqsanger.gz
	SRR28343253_1.fastq.gz	Fastqsanger.gz

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The HtrA chaperone monitors sortase-assembled pilus biogenesis in E. faecalis

Project description:Sortase-assembled pili contribute to virulence in many Gram-positive bacteria. In Enterococcus faecalis, the endocarditis and biofilm-associated pilus (Ebp) is polymerized on the membrane by sortase C (SrtC) and attached to the cell wall by sortase A (SrtA). In the absence of SrtA, polymerized pili remain anchored to the membrane (i.e. off-pathway). Here we show that the high temperature requirement A (HtrA) bifunctional chaperone/protease of E. faecalis is a quality control system that clears aberrant off-pathway pili from the cell membrane. In the absence of HtrA and SrtA, accumulation of membrane-bound pili leads to cell envelope stress and partially induces the regulon of the ceftriaxone resistance-associated CroRS two-component system, which in turn causes hyper-piliation and cell morphology alterations. Inactivation of croR in the ∆srtA∆htrA background partially restores the observed defects of the ∆srtA∆htrA strain, supporting a role for CroRS in the response to membrane perturbations. Moreover, absence of SrtA and HtrA decreases basal tolerance of E. faecalis against cephalosporins and daptomycin. The link between HtrA, pilus biogenesis and the CroRS two-component system provides new insights into the E. faecalis response to endogenous membrane perturbations.

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Structural basis of chaperone self-capping in P pilus biogenesis.

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Flagellar mutants have reduced pilus synthesis in Caulobacter crescentus

Project description:Surface appendages such as flagella and type IV pili mediate a broad range of bacterial behaviors including motility, attachment, and surface sensing. While many species harbor both flagella and type IV pili, little is known about how or if their synthesis is coupled. Here, we show that deletions of genes encoding different flagellum machinery components result in a reduction of pilus synthesis in Caulobacter crescentus. First, we show that different flagellar mutants exhibit different levels of sensitivity to a pilus-dependent phage and that less cells within populations of flagellar mutants make pili. Furthermore, we find that single cells within flagellar mutant populations produce less pili per cell. We demonstrate that these gene deletions result in reduced transcription of pilus-associated genes and have a broad effect on global transcription profiles. Finally, we show that the decrease in pilus production is due to a reduction in the pool of pilin subunits that are polymerized into pilus fibers. These data demonstrate that mutations in flagella gene components affect not only motility but can also have considerable and unexpected consequences on other aspects of cell biology.

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Comparative proteomic analysis of Neisseria meningitidis wildtype and dprA null mutant strains links DNA processing to pilus biogenesis

Project description:DNA processing chain A (DprA) is a DNA binding protein which is ubiquitous in bacteria and required for DNA transformation. However, the interaction of DprA with competence proteins and recombination is poorly understood. Therefore, the proteomes of whole Neisseria meningitidis (Nm) wildtype and dprA mutant cells were compared. Such a comparative proteomic analysis increases our understanding of the interactions of DprA with other Nm components, and may elucidate its potential role beyond DNA processing in transformation. Using label-free quantitative proteomics, a total of 1057 unique Nm proteins were identified out of which 100 were quantified as differentially abundant (P ≤ 0.05 and fold change ≥ |2|) in the dprA null mutant. Proteins involved in homologous recombination (RecA, UvrD and HolA), pilus biogenesis (PilG, PilT1, PilT2, PilM, PilO, PilQ, PilF and PilE), and cell division, including core energy metabolism and response to oxidative stress were downregulated in dprA null mutant Nm. Immunoblotting was employed to validate the differences observed in two selected proteins. The analysis revealed reduced amounts of PilG in the dprA null mutant and reduced amounts of DprA in the Nm pilG null mutant. In conclusion, DprA interacts with proteins essential for Nm DNA recombination in transformation, pilus biogenesis and other functions associated with the inner membrane. Inverse downregulation of Nm DprA and PilG expression in the corresponding mutants indicate a link between DNA processing and pilus biogenesis demonstrated for the first time.

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Project description:The High Temperature Requirement (HtrA) chaperone/protease is involved in the stress-response of the anthrax-causing pathogen Bacillus anthracis. Resilience to oxidative stress is essential for manifestation of B. anthracis pathogenicity. We submitt transcriptome data sets detailing global gene expression in B. anthracis wild-type and htrA-disrupted strains following H2O2-induced oxidative stress.

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PilY1 and minor pilins form a complex priming the type IVa pilus in Myxococcus xanthus

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