An enhancer sequence in the intrinsically disordered region of FtsZ promotes polymer-guided substrate processing by...

Area of Science:

• Microbiology
• Molecular Biology
• Biochemistry

Background:

• FtsZ is essential for bacterial cell division, forming the FtsZ-ring at midcell.
• A specific linker region in FtsZ was predicted to be intrinsically disordered and involved in filament organization.
• Most FtsZ-binding proteins interact with its polymerization or C-terminal domains, but ClpX interacts with the predicted disordered region.

Purpose of the Study:

• To investigate the structural nature of the FtsZ linker region.
• To elucidate the role of this intrinsically disordered region (IDR) in FtsZ function and degradation.
• To characterize the interaction between FtsZ's IDR and the ClpXP proteasome.

Main Methods:

• Nuclear Magnetic Resonance (NMR) spectroscopy was used to study the FtsZ linker region in solution.
• In vitro reconstituted degradation reactions were employed to assess FtsZ degradation.
• Polymerized FtsZ was used to study interactions with the ClpXP proteasome.

Main Results:

• NMR spectroscopy confirmed that the FtsZ linker region is intrinsically disordered in solution.
• The intrinsically disordered region (IDR) of FtsZ was found to enhance its degradation by the ClpXP proteasome.
• This enhancement occurs through polymer-guided interactions involving the IDR.

Conclusions:

• The linker region of FtsZ is intrinsically disordered and plays a role in modulating FtsZ filament architecture.
• The IDR of FtsZ mediates a secondary interaction with ClpX, the recognition component of the ClpXP proteasome.
• Amino acids within the FtsZ IDR enhance ClpXP-mediated degradation of FtsZ polymers.