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Related Experiment Video

Updated: May 20, 2026

Purification and Quality Control of Recombinant Septin Complexes for Cell-Free Reconstitution

Purification and Quality Control of Recombinant Septin Complexes for Cell-Free Reconstitution

Published on: June 23, 2022

Uncovering principles that control septin-septin interactions.

Moshe S Kim¹, Carol D Froese, Hong Xie

¹Program in Cell Biology, Department of Biochemistry, Hospital for Sick Children, University of Toronto, Toronto, Ontario M5G 1X8, Canada.

The Journal of Biological Chemistry

|July 21, 2012

Summary

Septins are proteins crucial for cell division. This study reveals that specific interactions at the G interface are essential before NC interface interactions can occur during septin filament formation.

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Published on: August 17, 2022

Area of Science:

Cell Biology
Molecular Biology
Biochemistry

Background:

Septins are a conserved family of GTPases essential for cytokinesis.
They assemble into filaments from heteromeric complexes, interacting via NC and G interfaces.

Purpose of the Study:

To investigate the roles of NC and G interfaces in septin filament formation.
To elucidate the sequential order of interface interactions during polymerization.

Main Methods:

Utilized N-terminal mutations in SEPT2 to induce homopolymer formation.
Examined filament formation using wild-type and mutated SEPT2 constructs (NC and G interface mutants).
Analyzed interactions between wild-type and mutant SEPT2 proteins.

Main Results:

Both NC and G interfaces are necessary for SEPT2 filament formation.
Mutations at the NC interface suppressed filament formation, while G interface mutations did not.
G interface mutants could still interact at NC interfaces, but NC mutants could not interact at G interfaces.
All promiscuous septin pairwise interactions occur at the G interface.

Conclusions:

The G interface interaction is a prerequisite for NC interface interaction during septin polymerization.
This finding clarifies the mechanism of septin filament assembly.