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Updated: May 14, 2026

Using a Bacterial Pathogen to Probe for Cellular and Organismic-level Host Responses

Using a Bacterial Pathogen to Probe for Cellular and Organismic-level Host Responses

Published on: February 22, 2019

FlgM proteins from different bacteria exhibit different structural characteristics.

Wai Kit Ma¹, Rachel Hendrix, Claire Stewart

¹Department of Chemistry and Biochemistry, Northern Arizona University, Flagstaff, AZ 86011, USA.

Biochimica Et Biophysica Acta

|January 29, 2013

Summary

Intrinsically disordered proteins (IDPs) like FlgM show varied structural conformations across species. This study reveals distinct disordered states in FlgM proteins, challenging the notion of universal conservation within protein families.

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Area of Science:

Protein structure and dynamics
Evolutionary biology
Biochemistry

Background:

Intrinsically disordered proteins (IDPs) lack stable structures but are crucial for biological functions.
The evolutionary conservation of disorder in protein families is not well understood.
FlgM proteins serve as a model system for studying IDP structural variations.

Purpose of the Study:

To investigate the structural diversity of orthologous FlgM proteins from different bacterial species.
To determine if the disordered state of FlgM is conserved across its evolutionary history.
To characterize the conformational states of FlgM proteins from Escherichia coli, Pseudomonas aeruginosa, Proteus mirabilis, and Bacillus subtilis.

Main Methods:

Comparative structural analysis of FlgM proteins.
Biophysical techniques to assess protein conformation (e.g., premolten globule, coil-like).
Analysis of intramolecular contacts and compaction states.

Main Results:

FlgM proteins from B. subtilis, E. coli, and S. typhimurium adopt a premolten globule-like conformation.
B. subtilis FlgM exhibits a more compact premolten globule state compared to E. coli and S. typhimurium.
P. aeruginosa and P. mirabilis FlgM proteins display unique, non-coil-like, non-premolten globule conformations.
P. aeruginosa FlgM shows greater compaction and more weak intramolecular contacts than P. mirabilis FlgM.

Conclusions:

The degree of intrinsic disorder varies significantly among orthologous FlgM proteins.
Different bacterial species have evolved distinct conformational states for the same protein family.
Further research is needed to understand the evolutionary mechanisms driving these diverse disordered states.