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The Contractile Ring

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...

The Contractile Ring

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...

Septins

Septins

Septins are protein filaments forming the cytoskeleton along with the microtubules, microfilaments, intermediate filaments, and other accessory proteins. In 1971 while studying the cell division cycle in mutant Saccharomyces cerevisiae Harwell et al. first identified the septin-related genes playing a crucial role in yeast cytokinesis. Fluorescence microscopy revealed that these proteins localize at the budding neck as rings. These ring-like proteins were then named Septins by John Pringle, and...

Role of Septins

Role of Septins

Septins are the recently discovered fourth major protein component of the cytoskeleton, along with microfilaments, microtubules, and intermediate filaments. These proteins can associate with other cytoskeletal filaments and carry out varied roles or can be free-floating in the cytoplasm.
Cellular Functions of Septins
Recent studies have revealed the multifaceted roles of septins in various cellular processes such as cytokinesis, ciliogenesis, and neurogenesis. Septins act as scaffolds and...

Ziegler–Natta Chain-Growth Polymerization: Overview

Ziegler–Natta Chain-Growth Polymerization: Overview

Ziegler–Natta polymerization is another form of addition or chain‐growth polymerization used for synthesizing linear polymers over branched polymers. The catalyst used for polymerization is the Ziegler–Natta catalyst, named after Karl Ziegler and Giulio Natta, who developed it in 1953. This catalyst is an organometallic complex of titanium tetrachloride and triethyl aluminum, with the active form of the catalyst being an alkyl titanium compound. Using the Ziegler–Natta catalyst, high molecular...

Actin Polymerization

Actin Polymerization

Actin polymerization occurs through the head-to-tail association of binding sites on monomeric actin or G-actin to form filamentous or F-actin. The polymerization can be divided into three phases ̶ nucleation, elongation, and steady-state phase.
The nucleation phase involves forming a stable nucleus consisting of three actin monomers to form a new actin filament. Actin-binding proteins such as formins and Arp2/3 complex help filament growth post-nucleation. The Formins form straight actin...

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Related Experiment Video

Updated: Jun 5, 2026

Spatiotemporal Analysis of Cytokinetic Events in Fission Yeast

Spatiotemporal Analysis of Cytokinetic Events in Fission Yeast

Published on: February 20, 2017

Large ring polymers align FtsZ polymers for normal septum formation.

Muhammet E Gündoğdu¹, Yoshikazu Kawai, Nada Pavlendova

¹Centre for Bacterial Cell Biology, Institute for Cell and Molecular Biosciences, Newcastle University, Newcastle, UK.

The EMBO Journal

|January 13, 2011

Summary

This summary is machine-generated.

SepF protein forms large rings that organize bacterial cell division protein FtsZ into regular structures. This organization is crucial for normal bacterial cell division and preventing deformed septa.

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Area of Science:

Microbiology
Cell Biology
Structural Biology

Background:

Bacterial cytokinesis relies on the FtsZ ring scaffold for cell division.
SepF protein is essential for normal cell division in Gram-positive bacteria and cyanobacteria.
The precise role of SepF in septum formation remains unclear.

Purpose of the Study:

To investigate the structural role of SepF in bacterial cell division.
To elucidate how SepF contributes to the formation of normal division septa.

Main Methods:

Electron microscopy (EM) was used to study SepF structure and FtsZ protofilament organization.
In vitro assays examined the interaction between SepF and FtsZ.
In vivo studies assessed the function of SepF mutants in cell division.

Main Results:

SepF self-assembles into large rings (approximately 50 nm in diameter).
SepF rings bundle FtsZ protofilaments into long, regular tubular structures.
SepF mutants defective in ring formation or FtsZ interaction fail to align FtsZ filaments and exhibit abnormal cell division.

Conclusions:

SepF rings are essential for the ordered arrangement of FtsZ filaments during bacterial cytokinesis.
Disruption of SepF-mediated FtsZ organization leads to deformed septal morphologies.
SepF plays a critical structural role in ensuring proper bacterial cell division.