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  1. Article ; Online: Flagellum and toxin phase variation impacts intestinal colonization and disease development in a mouse model of

    Trzilova, Dominika / Warren, Mercedes A H / Gadda, Nicole C / Williams, Caitlin L / Tamayo, Rita

    Gut microbes

    2022  Volume 14, Issue 1, Page(s) 2038854

    Abstract: Clostridioides ... ...

    Abstract Clostridioides difficile
    MeSH term(s) Animals ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Bacterial Toxins/genetics ; Bacterial Toxins/metabolism ; Clostridioides difficile/genetics ; Clostridium Infections/metabolism ; Cricetinae ; Disease Models, Animal ; Flagella/genetics ; Flagella/metabolism ; Gastrointestinal Microbiome ; Gene Expression Regulation, Bacterial ; Mice ; Phase Variation
    Chemical Substances Bacterial Proteins ; Bacterial Toxins
    Language English
    Publishing date 2022-02-22
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ISSN 1949-0984
    ISSN (online) 1949-0984
    DOI 10.1080/19490976.2022.2038854
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Coordinated modulation of multiple processes through phase variation of a c-di-GMP phosphodiesterase in Clostridioides difficile.

    Reyes Ruiz, Leila M / King, Kathleen A / Agosto-Burgos, Christian / Gamez, Isabella S / Gadda, Nicole C / Garrett, Elizabeth M / Tamayo, Rita

    PLoS pathogens

    2022  Volume 18, Issue 7, Page(s) e1010677

    Abstract: The opportunistic nosocomial pathogen Clostridioides difficile exhibits phenotypic heterogeneity through phase variation, a stochastic, reversible process that modulates expression. In C. difficile, multiple sequences in the genome undergo inversion ... ...

    Abstract The opportunistic nosocomial pathogen Clostridioides difficile exhibits phenotypic heterogeneity through phase variation, a stochastic, reversible process that modulates expression. In C. difficile, multiple sequences in the genome undergo inversion through site-specific recombination. Two such loci lie upstream of pdcB and pdcC, which encode phosphodiesterases (PDEs) that degrade the signaling molecule c-di-GMP. Numerous phenotypes are influenced by c-di-GMP in C. difficile including cell and colony morphology, motility, colonization, and virulence. In this study, we aimed to assess whether PdcB phase varies, identify the mechanism of regulation, and determine the effects on intracellular c-di-GMP levels and regulated phenotypes. We found that expression of pdcB is heterogeneous and the orientation of the invertible sequence, or 'pdcB switch', determines expression. The pdcB switch contains a promoter that when properly oriented promotes pdcB expression. Expression is augmented by an additional promoter upstream of the pdcB switch. Mutation of nucleotides at the site of recombination resulted in phase-locked strains with significant differences in pdcB expression. Characterization of these mutants showed that the pdcB locked-ON mutant has reduced intracellular c-di-GMP compared to the locked-OFF mutant, consistent with increased and decreased PdcB activity, respectively. These alterations in c-di-GMP had concomitant effects on multiple known c-di-GMP regulated processes, indicating that phase variation of PdcB allows C. difficile to coordinately diversify multiple phenotypes in the population to enhance survival.
    MeSH term(s) Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Biofilms ; Clostridioides difficile/enzymology ; Clostridioides difficile/genetics ; Cyclic GMP/analogs & derivatives ; Cyclic GMP/metabolism ; Gene Expression Regulation, Bacterial ; Phase Variation ; Phosphoric Diester Hydrolases/genetics ; Phosphoric Diester Hydrolases/metabolism
    Chemical Substances Bacterial Proteins ; bis(3',5')-cyclic diguanylic acid (61093-23-0) ; Phosphoric Diester Hydrolases (EC 3.1.4.-) ; Cyclic GMP (H2D2X058MU)
    Language English
    Publishing date 2022-07-05
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2205412-1
    ISSN 1553-7374 ; 1553-7374
    ISSN (online) 1553-7374
    ISSN 1553-7374
    DOI 10.1371/journal.ppat.1010677
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Micron-scale supramolecular myosin arrays help mediate cytoskeletal assembly at mature adherens junctions.

    Yu-Kemp, Hui-Chia / Szymanski, Rachel A / Cortes, Daniel B / Gadda, Nicole C / Lillich, Madeline L / Maddox, Amy S / Peifer, Mark

    The Journal of cell biology

    2021  Volume 221, Issue 1

    Abstract: Epithelial cells assemble specialized actomyosin structures at E-Cadherin-based cell-cell junctions, and the force exerted drives cell shape change during morphogenesis. The mechanisms that build this supramolecular actomyosin structure remain unclear. ... ...

    Abstract Epithelial cells assemble specialized actomyosin structures at E-Cadherin-based cell-cell junctions, and the force exerted drives cell shape change during morphogenesis. The mechanisms that build this supramolecular actomyosin structure remain unclear. We used ZO-knockdown MDCK cells, which assemble a robust, polarized, and highly organized actomyosin cytoskeleton at the zonula adherens, combining genetic and pharmacologic approaches with superresolution microscopy to define molecular machines required. To our surprise, inhibiting individual actin assembly pathways (Arp2/3, formins, or Ena/VASP) did not prevent or delay assembly of this polarized actomyosin structure. Instead, as junctions matured, micron-scale supramolecular myosin arrays assembled, with aligned stacks of myosin filaments adjacent to the apical membrane, overlying disorganized actin filaments. This suggested that myosin arrays might bundle actin at mature junctions. Consistent with this idea, inhibiting ROCK or myosin ATPase disrupted myosin localization/organization and prevented actin bundling and polarization. We obtained similar results in Caco-2 cells. These results suggest a novel role for myosin self-assembly, helping drive actin organization to facilitate cell shape change.
    MeSH term(s) Actin Cytoskeleton/metabolism ; Actin-Related Protein 2-3 Complex/metabolism ; Actins/metabolism ; Actomyosin/metabolism ; Adherens Junctions/metabolism ; Animals ; Caco-2 Cells ; Cytoskeleton/metabolism ; DNA-Binding Proteins ; Dogs ; Formins/metabolism ; Humans ; Madin Darby Canine Kidney Cells ; Models, Biological ; Myosin-Light-Chain Kinase/metabolism ; Myosins/metabolism ; rho-Associated Kinases/metabolism
    Chemical Substances Actin-Related Protein 2-3 Complex ; Actins ; DNA-Binding Proteins ; ENA-VASP proteins ; Formins ; Actomyosin (9013-26-7) ; rho-Associated Kinases (EC 2.7.11.1) ; Myosin-Light-Chain Kinase (EC 2.7.11.18) ; Myosins (EC 3.6.4.1)
    Language English
    Publishing date 2021-11-23
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 218154-x
    ISSN 1540-8140 ; 0021-9525
    ISSN (online) 1540-8140
    ISSN 0021-9525
    DOI 10.1083/jcb.202103074
    Database MEDical Literature Analysis and Retrieval System OnLINE

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