Home
Deutsch
Advanced Search
Browse by ...
Publication overview
Contact persons
Help
Publ. Version/Full Text
DOI
 |
Open Access Gold |
|
as soon as is submitted to ZB.
Crosslinking by ZapD drives the assembly of short FtsZ filaments into toroidal structures in solution.
eLife, DOI: 10.7554/elife.95557.2 (2025)
Bacterial cell division relies on the Z ring, a cytoskeletal structure
that acts as a scaffold for the assembly of the divisome. To date, the
detailed mechanisms underlying the assembly and stabilization of the Z
ring remain elusive. This study highlights the role of the
FtsZ-associated protein (Zap) ZapD in the assembly and stabilization of
Z-ring-like structures via filament crosslinking. Using cryo-electron
tomography and biochemical analysis, we show that, at equimolar
concentrations of ZapD and FtsZ, ZapD induces the formation of toroidal
structures composed of short, curved FtsZ filaments that are crosslinked
vertically, but also laterally and diagonally. At higher concentrations
of ZapD, regularly spaced ZapD dimers crosslink FtsZ filaments from
above, resulting in the formation of straight bundles. Despite the
simplicity of this reconstituted system, these findings provide valuable
insights into the structural organization and stabilization of the Z
ring by Zap proteins in bacterial cells, revealing the key role of
optimal crosslinking density and geometry in enabling filament curvature
and ring formation.
Altmetric
Additional Metrics?
Edit extra informations
Login
Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Ftsz
ISSN (print) / ISBN
2050-084X
e-ISSN
2050-084X
Journal
eLife
Publisher
eLife Sciences Publications
Non-patent literature
Publications
Reviewing status
Peer reviewed
Institute(s)
Helmholtz Pioneer Campus (HPC)