Polymerization of Ftsz, a bacterial homolog of tubulin. is assembly cooperative?

Published

Journal Article

FtsZ is a bacterial homolog of tubulin that is essential for prokaryotic cytokinesis. In vitro, GTP induces FtsZ to assemble into straight, 5-nm-wide polymers. Here we show that the polymerization of these FtsZ filaments most closely resembles noncooperative (or "isodesmic") assembly; the polymers are single-stranded and assemble with no evidence of a nucleation phase and without a critical concentration. We have developed a model for the isodesmic polymerization that includes GTP hydrolysis in the scheme. The model can account for the lengths of the FtsZ polymers and their maximum steady state nucleotide hydrolysis rates. It predicts that unlike microtubules, FtsZ protofilaments consist of GTP-bound FtsZ subunits that hydrolyze their nucleotide only slowly and are connected by high affinity longitudinal bonds with a nanomolar K(D).

Full Text

Duke Authors

Cited Authors

  • Romberg, L; Simon, M; Erickson, HP

Published Date

  • April 13, 2001

Published In

Volume / Issue

  • 276 / 15

Start / End Page

  • 11743 - 11753

PubMed ID

  • 11152458

Pubmed Central ID

  • 11152458

International Standard Serial Number (ISSN)

  • 0021-9258

Digital Object Identifier (DOI)

  • 10.1074/jbc.M009033200

Language

  • eng

Conference Location

  • United States