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Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins
Published on: September 23, 2021
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Are the curli proteins CsgE and CsgF intrinsically disordered?
Amanda Green1, Nguyen Pham1, Krystle Osby1
1Department of Chemistry and Biochemistry, California State University San Marcos , San Marcos, CA, USA.
Intrinsically Disordered Proteins
|February 25, 2017
Summary
Curli assembly proteins CsgE and CsgF from enteric bacteria are likely disordered. Sequence analysis and spectroscopy suggest these proteins lack stable structures, aiding curli filament formation.
Area of Science:
- Microbiology
- Structural Biology
- Biochemistry
Background:
- Curli are protein filaments on enteric bacteria surfaces, crucial for adhesion, invasion, and biofilm formation.
- Curli assembly involves six proteins, with CsgA as the main structural component.
- CsgE and CsgF are proposed to act as chaperones in CsgA assembly.
Purpose of the Study:
- To investigate if curli assembly proteins CsgE and CsgF possess disordered structures.
- To determine the structural characteristics of CsgE and CsgF in relation to their chaperone-like functions.
Main Methods:
- Sequence analysis, including charge-hydrophobicity assessment and PONDR disorder prediction.
- Circular dichroism (CD) spectroscopy to analyze secondary structure and unfolding.
Main Results:
- Sequence analysis indicated significant intrinsically disordered regions in both CsgE and CsgF.
- CD spectroscopy revealed that CsgE and CsgF lack well-defined, stable secondary structures.
Conclusions:
- The findings support the hypothesis that CsgE and CsgF are intrinsically disordered proteins.
- The disordered nature of CsgE and CsgF likely facilitates their chaperone-like roles in curli assembly.
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