FtsZ condensates: an in vitro electron microscopy study.

Journal Article

In vivo cell division protein FtsZ from E. coli forms rings and spirals which have only been observed by low resolution light microscopy. We show that these suprastructures are likely formed by molecular crowding which is a predominant factor in prokaryotic cells and enhances the weak lateral bonds between proto-filaments. Although FtsZ assembles into single proto-filaments in dilute aqueous buffer, with crowding agents above a critical concentration, it forms polymorphic supramolecular structures including rings and toroids (with multiple protofilaments) about 200 nm in diameter, similar in appearance to DNA toroids, and helices with pitches of several hundred nm as well as long, linear bundles. Helices resemble those observed in vivo, whereas the rings and toroids may represent a novel energy minimized state of FtsZ, at a later stage of Z-ring constriction. We shed light on the molecular arrangement of FtsZ filaments within these suprastructures using high resolution electron microscopy.

Full Text

Duke Authors

Cited Authors

  • Popp, D; Iwasa, M; Narita, A; Erickson, HP; Maéda, Y

Published Date

  • May 2009

Published In

Volume / Issue

  • 91 / 5

Start / End Page

  • 340 - 350

PubMed ID

  • 19137575

International Standard Serial Number (ISSN)

  • 0006-3525

Digital Object Identifier (DOI)

  • 10.1002/bip.21136

Language

  • eng

Conference Location

  • United States