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Showing 1 to 11 of 11 for “"FtsA"”.

  1. Characterization of ftsA conditional lethal mutants shows that FtsA is required at early and late stages of cell division in Streptococcus pneumoniae

    FtsA is an essential cell division protein fairly conserved among Eubacteria. It is an actin-like protein that structurally differs from actin because it lacks one of the four subdomains that is replaced by an additional one located elsewhere in the structure. FtsA localizes early at the cell …

    cagliari Repository record for Characterization of ftsA conditional lethal mutants shows that FtsA is required at early and late stages of cell division in Streptococcus pneumoniae (opens in a new tab)

  2. Characterization of Ftsa-Ftsn Interaction During Escherichia Coli Cell Division

    … of downstream cell division proteins including FtsA, a cytoplasmic protein that tethers the Z ring to the inner membrane. Following localization of FtsA and other early cell division proteins, a number of additional cell division proteins are recruited to midcell. The last essential cell …

    uthsc Repository record for Characterization of Ftsa-Ftsn Interaction During Escherichia Coli Cell Division (opens in a new tab)

  3. Functional Analysis of FtsA-Mediated Recruitment of FtsK in Escherichia coli

    … occur in synchrony. The actin-like protein FtsA plays a central role in this process by tethering FtsZ to the membrane and recruiting downstream division proteins. Despite its essential function, the mechanisms by which FtsA coordinates divisome activation and the recruitment of late-acting …

    uthsc Repository record for Functional Analysis of FtsA-Mediated Recruitment of FtsK in Escherichia coli (opens in a new tab)

  4. Regulators of Bacterial Cell Division: Investigations of Min Oscillation and Ftsa Activity

    … important for positioning of the divisome; and FtsA, involved in early and late stages of divisome formation with a speculated role in regulating its constriction and disassembly. In <em>E. coli</em> the Min proteins oscillate from pole-to-pole to prevent Z ring formation at the cell poles. I …

    uthsc Repository record for Regulators of Bacterial Cell Division: Investigations of Min Oscillation and Ftsa Activity (opens in a new tab)

  5. Biochemical and structural studies of the FtsZ:FtsA complex and polymerising abilities of the FtsA protein

    … this process, FtsZ is known to interact with FtsA, which is an early component of the Z-ring, and then recruits other components of the divisome, the cell division apparatus. Analysis of FtsA sequences revealed a conserved C-terminal motif, which is predicted to form an amphipathic helix and …

    cambridge Repository record for Biochemical and structural studies of the FtsZ:FtsA complex and polymerising abilities of the FtsA protein (opens in a new tab)

  6. The bacterial actin-like cell division protein FtsA forms antiparallel double filaments upon binding of FtsN

    … in the cytoplasm, the Z ring. Actin like FtsA tethers FtsZ to the inner membrane and facilitates recruitment of downstream divisome components. The late divisome component FtsN is a bitopic membrane protein that activates peptidoglycan synthesis. Recent genetic studies have suggested that …

    cambridge Repository record for The bacterial actin-like cell division protein FtsA forms antiparallel double filaments upon binding of FtsN (opens in a new tab)

  7. Organization and Regulation of Proteins Required For Initiation of Cell Division In Escherichia Coli

    … during synthesis of the division septum. Both FtsA, a bacterial homolog of eukaryotic actin, and ZipA, a single-pass transmembrane protein, anchor the Z ring to the inner membrane, are required for the localization of other divisome proteins to midcell, and likely influence the assembly state …

    uthsc Repository record for Organization and Regulation of Proteins Required For Initiation of Cell Division In Escherichia Coli (opens in a new tab)

  8. Mutations Within and Between Early Cell Division Proteins and Their Effects On Division Regulation In Escherichia Coli

    … proteins: FtsZ and its membrane tethers FtsA and ZipA. In this work, I aimed to understand the early regulation of division in E. coli by investigating the structure/function relationships of the proto-ring proteins, as well as their interactions with one another and how these influence …

    uthsc Repository record for Mutations Within and Between Early Cell Division Proteins and Their Effects On Division Regulation In Escherichia Coli (opens in a new tab)

  9. Genetically encoded division machinery for cell free synthetic biology

    … interactions with the membrane are mediated by FtsA and ZipA. Therefore, the influence of FtsA on the behavior of FtsZ also was investigated. Fluorescently tagged constructs were used to facilitate evaluation by microscopy. The data showed that FtsZ readily assembles into rings in the presence …

    trento Repository record for Genetically encoded division machinery for cell free synthetic biology (opens in a new tab)

  10. Analysis of TpeL secretion in Clostridium perfringens

    … by alternatively associating with PilM and FtsA. We developed an experimental plan to determine if PilT binds both PilM and FtsA by co-immunoprecipitation with live-cell fluorescence imaging. However, we were unable to demonstrate the functionality of a PilT-fluorescent protein fusion with …

    vt Repository record for Analysis of TpeL secretion in Clostridium perfringens (opens in a new tab)

  11. Escherichia coli and Rhizobium leguminosarum response mechanisms to sub-lethal 2,4-dichlorophenoxyacetic acid

    … mechanistic level, 2,4-D at >1 mM altered FtsZ, FtsA and SulA localization within seconds accompanied by DNA damage resulting in immediate inhibition of Z-ring formation and arrest of cell division. There were simultaneous changes to cell surface roughness, elasticity and adhesion in a …

    regina Repository record for Escherichia coli and Rhizobium leguminosarum response mechanisms to sub-lethal 2,4-dichlorophenoxyacetic acid (opens in a new tab)