Combined analytical ultracentrifugation, light scattering and fluorescence spectroscopy studies on the functional associations of the bacterial division FtsZ protein.

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  • Author(s): Monterroso B;Monterroso B; Alfonso C; Zorrilla S; Rivas G
  • Source:
    Methods (San Diego, Calif.) [Methods] 2013 Mar; Vol. 59 (3), pp. 349-62. Date of Electronic Publication: 2013 Jan 05.
  • Publication Type:
    Journal Article; Research Support, Non-U.S. Gov't; Review
  • Language:
    English
  • Additional Information
    • Source:
      Publisher: Academic Press Country of Publication: United States NLM ID: 9426302 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1095-9130 (Electronic) Linking ISSN: 10462023 NLM ISO Abbreviation: Methods Subsets: MEDLINE
    • Publication Information:
      Publication: Duluth, MN : Academic Press
      Original Publication: San Diego : Academic Press, c1990-
    • Subject Terms:
      Bacterial Proteins/*chemistry ; Cytoskeletal Proteins/*chemistry ; Spectrometry, Fluorescence/*methods ; Ultracentrifugation/*methods; Bacterial Proteins/metabolism ; Cytoskeletal Proteins/metabolism ; Light ; Scattering, Radiation
    • Abstract:
      The combined application of different biophysical techniques - analytical ultracentrifugation, light scattering and fluorescence-based assays - to study the ligand-linked self-association and assembly properties of the cell division protein FtsZ from Escherichia coli is described. These reactions are thought to be important for the formation of the dynamic division ring that drives bacterial cytokinesis. In addition, the use of this orthogonal experimental approach to measure the interactions between FtsZ oligomers (GDP forms) and polymers (GTP forms) with two variants (a soluble form and a full-length protein incorporated in phospholipid bilayer nanodiscs) of the ZipA protein, which provides membrane tethering to FtsZ, is described as well. The power of a global analysis of the results obtained from complementary biophysical methods to discriminate among alternative self- and hetero-associating schemes and to propose a more robust description of the association reactions involved is emphasized. This orthogonal approach will contribute to complete our quantitative understanding of the initial events of bacterial division.
      (Copyright © 2013 Elsevier Inc. All rights reserved.)
    • Accession Number:
      0 (Bacterial Proteins)
      0 (Cytoskeletal Proteins)
      0 (FtsZ protein, Bacteria)
    • Publication Date:
      Date Created: 20130109 Date Completed: 20130923 Latest Revision: 20130325
    • Publication Date:
      20221213
    • Accession Number:
      10.1016/j.ymeth.2012.12.014
    • Accession Number:
      23296019