MinCD cell division proteins form alternating copolymeric cytomotive filaments

Related Experiment Video

Updated: Apr 19, 2026

Combining Mitotic Cell Synchronization and High Resolution Confocal Microscopy to Study the Role of Multifunctional Cell Cycle Proteins During Mitosis
08:33

Combining Mitotic Cell Synchronization and High Resolution Confocal Microscopy to Study the Role of Multifunctional Cell Cycle Proteins During Mitosis

Published on: December 5, 2017

15.1K

Debnath Ghosal1, Daniel Trambaiolo1, Linda A Amos1

  • 1Structural Studies, MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK.

Nature Communications
|December 16, 2014
PubMed

Insights

Bacterial cell division relies on FtsZ ring formation, regulated by MinCDE proteins. Researchers discovered MinD activates MinC by forming novel copolymer filaments, crucial for precise Z-ring placement during cell division.

Area of Science:

  • Microbiology
  • Cell Biology
  • Structural Biology

Background:

  • Bacterial cell division requires the FtsZ protein to form a cytokinetic Z-ring at midcell.
  • The MinCDE protein system regulates Z-ring positioning, with MinC inhibiting assembly outside midcell.
  • The mechanism of MinD-mediated MinC activation remained unknown.

Purpose of the Study:

  • To elucidate the mechanism by which MinD activates MinC.
  • To understand the structural basis of MinCD interaction and its role in bacterial cytokinesis.
  • To investigate the regulation of FtsZ ring assembly by the MinCD system.

Main Methods:

  • X-ray crystallography to determine protein structures.
  • Electron microscopy for visualizing filament formation and interactions.
  • In vivo analyses in Escherichia coli, including mutational studies.
  • Liposome-based reconstitution assays to study MinCD-FtsZ interactions.

Main Results:

  • MinD activates MinC by forming a novel class of alternating copolymeric filaments, structurally similar to eukaryotic septins.
  • A mutation in MinD preventing polymerization led to aberrant cell division in E. coli.
  • MinCD copolymers bind to membranes, interact with FtsZ, and are disassembled by MinE.
  • Imaging revealed filamentous MinC structures in vivo and MinCD-FtsZ interactions on liposomes.

Conclusions:

  • MinD activates MinC through copolymer filament formation, a mechanism distinct from previously known protein activation pathways.
  • These MinCD copolymers play a critical role in correctly positioning the FtsZ ring, ensuring proper bacterial cell division.
  • The findings provide a structural and mechanistic basis for MinCDE-mediated spatial regulation of cytokinesis.

More Related Videos

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay12:26

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay

Published on: May 3, 2018

19.5K
Spatiotemporal Analysis of Cytokinetic Events in Fission Yeast11:19

Spatiotemporal Analysis of Cytokinetic Events in Fission Yeast

Published on: February 20, 2017

7.8K

Related Concept Videos

The Contractile Ring02:15

The Contractile Ring

Contractile rings are composed of microfilaments and are responsible for separating the daughter cells during cytokinesis. Contractile ring assembly proceeds along with other cell cycle events; however, very few mechanistic details are known about the timing and coordination of the contractile rings with the cell cycle.
A small GTPase, RhoA, controls the function and assembly of the contractile ring. RhoA belongs to the Ras superfamily of proteins. The activation of formins by RhoA promotes...
7.5K
The Contractile Ring02:15

The Contractile Ring

3.2K
M-Cdk Drives Transition Into Mitosis02:15

M-Cdk Drives Transition Into Mitosis

Checkpoints throughout the cell cycle serve as safeguards and gatekeepers, allowing the cell cycle to progress in favorable conditions and slow or halt it in problematic ones. This regulation is known as the cell cycle control system.
Cyclin-dependent kinases, or Cdks, work in concert with cyclins to control cell cycle transitions. M-Cdk, a complex of Cdk1 bound to M cyclin, is a well-known example of this coordinated control that drives the transition from the G2 to the M phase.
M cyclin...
6.8K
M-Cdk Drives Transition Into Mitosis02:15

M-Cdk Drives Transition Into Mitosis

3.1K
Separation of Sister Chromatids02:17

Separation of Sister Chromatids

At the transition from prophase to metaphase, there is a reduction in cohesion along the chromosomal arms, resulting in the resolution of sister chromatids. However, residual cohesin connections remain to hold the sister chromatids together until the transition from metaphase to anaphase. The residual connection prevents any premature separation of sister chromatids, blocking the risks of aneuploidy within the daughter cells.
At the onset of anaphase, separase, a proteolytic enzyme, is...
4.8K
Adaptability of Cytoskeletal Filaments01:12

Adaptability of Cytoskeletal Filaments

The cytoskeleton is a complex dynamic structure performing varied functions based on cellular requirements. The adaptability of the individual filaments in the cytoskeleton determines their ability to perform various functions within the cell. It can undergo rapid reorganization during processes like cell division or remain stable for several hours as in the interphase. The adaptability of these filaments depends on stringent regulatory mechanisms. The microfilament and microtubules of the...
6.9K