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FlgM gains structure in living cells.
Matthew M Dedmon1, Chetan N Patel, Gregory B Young
1Departments of Chemistry, and Biochemistry and Biophysics, and Lineberger Cancer Research Center, University of North Carolina, Chapel Hill, NC 27599, USA.
Summary
Intrinsically disordered proteins like FlgM gain structure within living bacterial cells and in concentrated solutions. This highlights how cellular environments influence protein structure and function.
Area of Science:
- Biochemistry
- Molecular Biology
- Structural Biology
Background:
- Intrinsically disordered proteins (IDPs) are crucial in biological processes.
- The in-cell structure of IDPs remains largely uncharacterized.
- FlgM is an example of an IDP with unknown cellular structure.
Purpose of the Study:
- To investigate the structural behavior of FlgM within living Escherichia coli cells.
- To determine if FlgM adopts a structured state under physiologically relevant conditions in vitro.
- To understand the influence of cellular environments on IDP structure.
Main Methods:
- Nuclear Magnetic Resonance (NMR) spectroscopy was employed.
- Experiments were conducted in vivo within living E. coli.
- In vitro studies used high concentrations of solutes like glucose, BSA, and ovalbumin.
Main Results:
- FlgM was observed to gain structure inside living E. coli cells.
- High concentrations of glucose, BSA, or ovalbumin induced structure formation in FlgM in vitro.
- Structure acquisition is attributed to solute-induced shifts in the protein's conformational equilibrium.
Conclusions:
- The cellular environment significantly impacts the structure of intrinsically disordered proteins.
- Physiologically relevant conditions, including high solute concentrations, can induce structure in IDPs.
- Studying proteins in vivo and under realistic in vitro conditions is essential for understanding their function.