Intrinsically Disordered to α-Helix Transition of the IM30 Protein Structure (R01)

• Subject Area: Biochemistry
• Term: since 2023
• Project identifier: Deutsche Forschungsgemeinschaft (DFG) - Project number 464588647

In eukaryotes, several membrane remodeling processes involve ESCRT-III proteins, which are also conserved in bacteria. Monomers of the bacterial ESCRT-III superfamily member IM30 assemble to form large homo-oligomeric barrel structures, where the monomers are ~80% α‑helical. Upon membrane binding, these barrels disassemble, and the C-terminal part of monomeric IM30 unfolds. In solution, oligomerization-impaired IM30 forms liquid condensates by a phase separation process. We will study the α‑helix-to-disordered structural transition of IM30 in solution as well as on membranes surfaces, using a combination of molecular dynamics simulations, biochemical and biophysical analyses.

• DFG Programme: Collaborative Research Centres
• Subproject of: SFB 1551: Polymer Concepts in Cellular Function
• Applicant Institution: Johannes Gutenberg-Universität Mainz
• Project Heads: Professor Dr. Mischa Bonn; Dr. Martin Girard; Professor Dr. Dirk Schneider