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The C-terminal linker of Escherichia coli FtsZ functions as an intrinsically disordered peptide.

Publication ,  Journal Article
Gardner, KAJA; Moore, DA; Erickson, HP
Published in: Mol Microbiol
July 2013

The tubulin homologue FtsZ provides the cytoskeletal framework and constriction force for bacterial cell division. FtsZ has an 50-amino-acid (aa) linker between the protofilament-forming globular domain and the C-terminal (Ct) peptide that binds FtsA and ZipA, tethering FtsZ to the membrane. This Ct-linker is widely divergent across bacterial species and thought to be an intrinsically disordered peptide (IDP). We confirmed that the Ct-linkers from three bacterial species behaved as IDPs in vitro by circular dichroism and trypsin proteolysis. We made chimeras, swapping the Escherichia coli linker for Ct-linkers from other bacteria, and even for an unrelated IDP from human α-adducin. Most substitutions allowed for normal cell division, suggesting that sequence of the IDP did not matter. With few exceptions, almost any sequence appears to work. Length, however, was important: IDPs shorter than 43 or longer than 95 aa had compromised or no function. We conclude that the Ct-linker functions as a flexible tether between the globular domain of FtsZ in the protofilament, and its attachment to FtsA/ZipA at the membrane. Modelling the Ct-linker as a worm-like chain, we predict that it functions as a stiff entropic spring linking the bending protofilaments to the membrane.

Duke Scholars

Published In

Mol Microbiol

DOI

EISSN

1365-2958

Publication Date

July 2013

Volume

89

Issue

2

Start / End Page

264 / 275

Location

England

Related Subject Headings

  • Protein Conformation
  • Protein Binding
  • Peptides
  • Models, Molecular
  • Microbiology
  • Humans
  • Escherichia coli Proteins
  • Escherichia coli
  • Cytoskeletal Proteins
  • Cell Division
 

Citation

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Gardner, K. A. J. A., Moore, D. A., & Erickson, H. P. (2013). The C-terminal linker of Escherichia coli FtsZ functions as an intrinsically disordered peptide. Mol Microbiol, 89(2), 264–275. https://doi.org/10.1111/mmi.12279
Gardner, Kiani AJ Arkus, Desmond A. Moore, and Harold P. Erickson. “The C-terminal linker of Escherichia coli FtsZ functions as an intrinsically disordered peptide.Mol Microbiol 89, no. 2 (July 2013): 264–75. https://doi.org/10.1111/mmi.12279.
Gardner KAJA, Moore DA, Erickson HP. The C-terminal linker of Escherichia coli FtsZ functions as an intrinsically disordered peptide. Mol Microbiol. 2013 Jul;89(2):264–75.
Gardner, Kiani AJ Arkus, et al. “The C-terminal linker of Escherichia coli FtsZ functions as an intrinsically disordered peptide.Mol Microbiol, vol. 89, no. 2, July 2013, pp. 264–75. Pubmed, doi:10.1111/mmi.12279.
Gardner KAJA, Moore DA, Erickson HP. The C-terminal linker of Escherichia coli FtsZ functions as an intrinsically disordered peptide. Mol Microbiol. 2013 Jul;89(2):264–275.
Journal cover image

Published In

Mol Microbiol

DOI

EISSN

1365-2958

Publication Date

July 2013

Volume

89

Issue

2

Start / End Page

264 / 275

Location

England

Related Subject Headings

  • Protein Conformation
  • Protein Binding
  • Peptides
  • Models, Molecular
  • Microbiology
  • Humans
  • Escherichia coli Proteins
  • Escherichia coli
  • Cytoskeletal Proteins
  • Cell Division