PUBLICATION
Cooperative unfolding of a single-layer β-sheet protein, CPAP G-box
- Authors
- Fujiwara, H., Shiga, S., Makabe, K.
- ID
- ZDB-PUB-201125-10
- Date
- 2020
- Source
- Biochemical and Biophysical Research Communications 526: 105-109 (Journal)
- Registered Authors
- Keywords
- CPAP G-box/TCP domain, Single-layer ?-sheet (SLB)
- MeSH Terms
-
- Zebrafish/metabolism*
- Protein Structure, Secondary
- Sequence Deletion
- Microtubule-Associated Proteins/chemistry*
- Protein Denaturation
- Animals
- Protein Domains
- Protein Stability
- Protein Unfolding*
- Zebrafish Proteins/chemistry*
- PubMed
- 32197835 Full text @ Biochem. Biophys. Res. Commun.
Citation
Fujiwara, H., Shiga, S., Makabe, K. (2020) Cooperative unfolding of a single-layer β-sheet protein, CPAP G-box. Biochemical and Biophysical Research Communications. 526:105-109.
Abstract
CPAP is a centriolar protein and its C-terminal domain, G-box or TCP, has a very unique structure that comprises a single-layer β-sheet without hydrophobic core packing. Here we characterized its biophysical properties, including its stability against chemical denaturation. Interestingly, upon urea-induced equilibrium unfolding, the CPAP G-box showed cooperative unfolding behavior that is the hallmark of globular proteins. We analyzed the m-value, a measure of the cooperative transition, from the urea-induced unfolding and found that the estimated m-value from surface burial upon folding is consistent with the experimental value, supporting the two-state unfolding. Next, we constructed deletion mutants of the terminal β-strands and found that the mutants showed reduced stability. The unique structure and characteristics of CPAP G-box provides an interesting opportunity to observe how the core-less flat β-sheet protein can be folded in solution.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping