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Updated: Aug 1, 2025

Purification and Quality Control of Recombinant Septin Complexes for Cell-Free Reconstitution
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Dissecting the Binding Interface of the Septin Polymerization Enhancer Borg BD3.

Danielle K S V Castro1, Higor V D Rosa2, Deborah C Mendonça2

  • 1São Carlos Institute of Chemistry, University of São Paulo, São Carlos, Brazil; São Carlos Institute of Physics, University of São Paulo, São Carlos, Brazil.

Journal of Molecular Biology
|April 30, 2023
PubMed
Summary

Septin C-terminal domains are crucial for filament assembly and binding Borg proteins. This interaction stabilizes septin complexes, promoting filament formation under specific conditions.

Keywords:
BD3-motifBorg’scoiled coilpolymerizationseptin

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Protein Interactions

Background:

  • Septin filaments are essential for various cellular functions, often requiring interaction with membranes or cytoskeleton.
  • The precise mechanisms by which septins interact with their binding partners remain largely unknown.

Purpose of the Study:

  • To elucidate the role of C-terminal domains in septin polymerization.
  • To characterize the molecular interaction between septins and the BD3 motif of Borg proteins.
  • To understand how binding partners influence septin filament assembly.

Main Methods:

  • Detailed molecular-level description of the BD3-septin interaction.
  • Analysis of ternary complex formation involving SEPT6, SEPT7, and BD3.
  • Experimental validation of structural models.

Main Results:

  • The C-terminal domains of septins are essential for polymerization and Borg BD3 motif association.
  • Ternary complex formation stabilizes the septin heterodimeric coiled coil.
  • Borg proteins promote septin filament assembly under non-permissive ionic conditions, favoring hexamers.
  • Structural models reveal antiparallel positioning of BD3 to the coiled coil, stabilized by polar and apolar contacts.
  • A conserved LGPS motif in Borg proteins interacts with charged residues in SEPT6 and SEPT7, indicating a universal binding mechanism.

Conclusions:

  • Septin C-terminal domains are key regulators of both polymerization and binding to Borg proteins.
  • Borg proteins can modulate septin filament assembly and disassembly in vivo.
  • A conserved molecular mechanism governs Borg-septin interactions, involving specific charge and hydrophobic contacts.