6 results found
    1. Biochemistry and Chemical Biology
    2. Structural Biology and Molecular Biophysics

    Mechanochemical coupling and bi-phasic force-velocity dependence in the ultra-fast ring ATPase SpoIIIE

    Ninning Liu et al.
    Probing the DNA motor SpoIIIE at the single-molecule level has revealed its force-generating step, rich translocation dynamics during motor operation and a novel, bi-phasic mechanical response to opposing force.
    1. Structural Biology and Molecular Biophysics

    Two-subunit DNA escort mechanism and inactive subunit bypass in an ultra-fast ring ATPase

    Ninning Liu et al.
    The subunits of the SpoIIIE motor contact the 5'→3' strand of DNA in sequence to rapidly translocate the DNA across a membrane.
    1. Microbiology and infectious disease

    Asymmetric division triggers cell-specific gene expression through coupled capture and stabilization of a phosphatase

    Niels Bradshaw, Richard Losick
    Asymmetric cell division is linked to cell-specific transcription by handoff of a key developmental regulator from the cytokinetic machinery to the adjacent cell pole where it oligomerizes to become stabilized and activated.
    1. Genetics and Genomics
    2. Microbiology and Infectious Disease

    Extensive horizontal gene transfer in cheese-associated bacteria

    Kevin S Bonham et al.
    The identification of horizontally transferred genes, and commonly transferred functions, can provide a window into the selective forces acting on species within an ecosystem.
    1. Structural Biology and Molecular Biophysics
    2. Cell Biology

    Visualization and functional dissection of coaxial paired SpoIIIE channels across the sporulation septum

    Jae Yen Shin et al.
    SpoIIIE forms a protein channel that spans the two lipid bilayers of the septum and mediates chromosome translocation and reversible membrane fission during Bacilus subtilis sporulation.
    1. Biochemistry and Chemical Biology
    2. Microbiology and Infectious Disease

    A widespread family of serine/threonine protein phosphatases shares a common regulatory switch with proteasomal proteases

    Niels Bradshaw et al.
    Structures of active and inactive conformations of a PP2C family phosphatase reveal a conserved switch that controls enzymatic activity and point to an unexpected relationship between phosphatases and proteasomal proteases.

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