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Inside-out Z rings--constriction with and without GTP hydrolysis.

Publication ,  Journal Article
Osawa, M; Erickson, HP
Published in: Mol Microbiol
July 2011

The bacterial tubulin homologue FtsZ forms a ring-like structure called the Z ring that drives cytokinesis. We showed previously that FtsZ-YFP-mts, which has a short amphipathic helix (mts) on its C terminus that inserts into the membrane, can assemble contractile Z rings in tubular liposomes without any other protein. Here we study mts-FtsZ-YFP, where the membrane tether is switched to the opposite side of the protofilament. This assembled 'inside-out' Z rings that wrapped around the outside surface of tubular liposomes. The inside-out Z rings were highly dynamic, and generated a constriction force that squeezed the tubular liposomes from outside. This is consistent with models where the constriction force is generated by curved protofilaments bending the membrane. We used this system to test how GTP hydrolysis by FtsZ is involved in Z-ring constriction. Without GTP hydrolysis, Z rings could still assemble and generate an initial constriction. However, the constriction quickly stopped, suggesting that Z rings became rigidly stabilized in the absence of GTP hydrolysis. We propose that remodelling of the Z ring, mediated by GTP hydrolysis and exchange of subunits, is necessary for the continuous constriction.

Duke Scholars

Published In

Mol Microbiol

DOI

EISSN

1365-2958

Publication Date

July 2011

Volume

81

Issue

2

Start / End Page

571 / 579

Location

England

Related Subject Headings

  • Protein Multimerization
  • Models, Molecular
  • Models, Chemical
  • Models, Biological
  • Microbiology
  • Liposomes
  • Hydrolysis
  • Guanosine Triphosphate
  • Cytoskeletal Proteins
  • Bacterial Proteins
 

Citation

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ICMJE
MLA
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Osawa, M., & Erickson, H. P. (2011). Inside-out Z rings--constriction with and without GTP hydrolysis. Mol Microbiol, 81(2), 571–579. https://doi.org/10.1111/j.1365-2958.2011.07716.x
Osawa, Masaki, and Harold P. Erickson. “Inside-out Z rings--constriction with and without GTP hydrolysis.Mol Microbiol 81, no. 2 (July 2011): 571–79. https://doi.org/10.1111/j.1365-2958.2011.07716.x.
Osawa M, Erickson HP. Inside-out Z rings--constriction with and without GTP hydrolysis. Mol Microbiol. 2011 Jul;81(2):571–9.
Osawa, Masaki, and Harold P. Erickson. “Inside-out Z rings--constriction with and without GTP hydrolysis.Mol Microbiol, vol. 81, no. 2, July 2011, pp. 571–79. Pubmed, doi:10.1111/j.1365-2958.2011.07716.x.
Osawa M, Erickson HP. Inside-out Z rings--constriction with and without GTP hydrolysis. Mol Microbiol. 2011 Jul;81(2):571–579.
Journal cover image

Published In

Mol Microbiol

DOI

EISSN

1365-2958

Publication Date

July 2011

Volume

81

Issue

2

Start / End Page

571 / 579

Location

England

Related Subject Headings

  • Protein Multimerization
  • Models, Molecular
  • Models, Chemical
  • Models, Biological
  • Microbiology
  • Liposomes
  • Hydrolysis
  • Guanosine Triphosphate
  • Cytoskeletal Proteins
  • Bacterial Proteins