PUBLICATION
Effect of calcium ions on structure and stability of the C1q-like domain of otolin-1 from human and zebrafish
- Authors
- Hołubowicz, R., Wojtas, M., Taube, M., Kozak, M., Ożyhar, A., Dobryszycki, P.
- ID
- ZDB-PUB-171028-3
- Date
- 2017
- Source
- The FEBS journal 284(24): 4278-4297 (Journal)
- Registered Authors
- Keywords
- SAXS, analytical ultracentrifugation, calcium binding protein, otolin-1, structural change
- MeSH Terms
-
- Amino Acid Sequence
- Animals
- Calcium/pharmacology*
- Calcium/physiology
- Chromatography, Gel
- Crystallography, X-Ray
- Extracellular Matrix Proteins/chemistry*
- Extracellular Matrix Proteins/drug effects
- Extracellular Matrix Proteins/isolation & purification
- Humans
- Models, Molecular
- Otolithic Membrane/metabolism
- Protein Conformation
- Protein Denaturation
- Protein Domains
- Protein Stability/drug effects
- Protein Structure, Secondary/drug effects
- Recombinant Fusion Proteins/chemistry
- Recombinant Fusion Proteins/drug effects
- Scattering, Radiation
- Sequence Alignment
- Sequence Homology, Amino Acid
- Species Specificity
- Structure-Activity Relationship
- Ultracentrifugation
- Zebrafish Proteins/chemistry*
- Zebrafish Proteins/drug effects
- Zebrafish Proteins/isolation & purification
- PubMed
- 29076638 Full text @ FEBS J.
Citation
Hołubowicz, R., Wojtas, M., Taube, M., Kozak, M., Ożyhar, A., Dobryszycki, P. (2017) Effect of calcium ions on structure and stability of the C1q-like domain of otolin-1 from human and zebrafish. The FEBS journal. 284(24):4278-4297.
Abstract
Otolin-1 is a collagen-like protein expressed in the inner ear of vertebrates. It provides an organic scaffold for otoliths in fish and otoconia in land vertebrates. In this study, the expression and purification procedure of C1q-like domain of otolin-1 from human and zebrafish was developed. The structure and stability of the proteins were investigated. The results of sedimentation velocity analytical ultracentrifugation and small angle X-ray scattering indicated that the C1q-like domain of otolin-1 forms stable trimers in solution in the presence of calcium ions. It was also observed that calcium ions influenced the secondary structure of the proteins. C1q-like domains were stabilized by the calcium ions. The human variant was especially affected by the calcium ions. The results indicate the importance of the C1q-like domain for the assembly of the organic matrix of otoliths and otoconia. This article is protected by copyright. All rights reserved.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping