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Regular surface layer of Azotobacter vinelandii.

W H Bingle, J L Doran, W J Page

    Journal of Bacteriology
    |July 1, 1984
    PubMed
    Summary

    The surface layer of Azotobacter vinelandii UW1 is formed by an S protein, which reassembles into a tetragonal array with specific cations. This protein

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    Area of Science:

    • Microbiology
    • Structural Biology
    • Biochemistry

    Background:

    • Azotobacter vinelandii UW1 possesses a surface layer.
    • The structure and composition of this layer are not fully understood.

    Purpose of the Study:

    • To investigate the composition and assembly of the Azotobacter vinelandii UW1 surface layer.
    • To identify the protein responsible for the surface layer structure and its assembly mechanism.

    Main Methods:

    • Freeze-etch electron microscopy to visualize the surface layer.
    • Cell washing protocols to isolate surface components.
    • Cation-mediated reattachment assays to study protein assembly.

    Main Results:

    • A regular tetragonal surface layer with 10 nm spacing was observed via electron microscopy.
    • Distilled water washing removed an acidic 65,000 MW outer membrane protein (S protein).
    • The S protein reattached to washed cells and formed tetragonal arrays in the presence of Ca2+, Mg2+, and Sr2+.

    Conclusions:

    • The S protein is the major component of the Azotobacter vinelandii UW1 surface layer.
    • The S protein self-assembles into a tetragonal array, dependent on specific divalent cations.
    • The surface localization of the S protein was confirmed, despite variable radioiodination results.

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