PUBLICATION
Effect of calcium ions on structure and stability of the C1q-like domain of otolin-1 from human and zebrafish
- Authors
- Ho?ubowicz, R., Wojtas, M., Taube, M., Kozak, M., O?yhar, 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
-
- Structure-Activity Relationship
- Crystallography, X-Ray
- Sequence Homology, Amino Acid
- Protein Conformation
- Animals
- Calcium/pharmacology*
- Calcium/physiology
- Scattering, Radiation
- Protein Structure, Secondary/drug effects
- Zebrafish Proteins/chemistry*
- Zebrafish Proteins/drug effects
- Zebrafish Proteins/isolation & purification
- Species Specificity
- Models, Molecular
- Protein Domains
- Humans
- Recombinant Fusion Proteins/chemistry
- Recombinant Fusion Proteins/drug effects
- Protein Stability/drug effects
- Extracellular Matrix Proteins/chemistry*
- Extracellular Matrix Proteins/drug effects
- Extracellular Matrix Proteins/isolation & purification
- Protein Denaturation
- Otolithic Membrane/metabolism
- Ultracentrifugation
- Sequence Alignment
- Amino Acid Sequence
- Chromatography, Gel
- PubMed
- 29076638 Full text @ FEBS J.
Citation
Ho?ubowicz, R., Wojtas, M., Taube, M., Kozak, M., O?yhar, 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