Zebavidin - an avidin-like protein from zebrafish
- Authors
- Taskinen, B., Zmurko, J., Ojanen, M., Kukkurainen, S., Parthiban, M., Määttä, J.A., Leppiniemi, J., Jänis, J., Parikka, M., Turpeinen, H., Rämet, M., Pesu, M., Johnson, M.S., Kulomaa, M.S., Airenne, T.T., and Hytönen, V.P.
- ID
- ZDB-PUB-131204-14
- Date
- 2013
- Source
- PLoS One 8(10): e77207 (Journal)
- Registered Authors
- Keywords
- none
- MeSH Terms
-
- Sequence Homology, Amino Acid
- Zebrafish/embryology
- Zebrafish/genetics*
- Zebrafish/metabolism
- Protein Binding
- Gonads/embryology
- Gonads/metabolism
- Protein Multimerization
- Female
- Biotin/chemistry
- Biotin/metabolism
- Molecular Sequence Data
- Gene Expression
- Avidin/chemistry*
- Avidin/genetics
- Avidin/metabolism
- Gills/embryology
- Gills/metabolism
- Models, Molecular
- Zebrafish Proteins/chemistry*
- Zebrafish Proteins/genetics
- Zebrafish Proteins/metabolism
- Embryo, Nonmammalian
- Animals
- Amino Acid Sequence
- Recombinant Proteins/chemistry
- Recombinant Proteins/genetics
- Recombinant Proteins/metabolism
- Glycoproteins/chemistry*
- Glycoproteins/genetics
- Glycoproteins/metabolism
- Genome*
- Escherichia coli/genetics
- Escherichia coli/metabolism
- Male
- Protein Isoforms/chemistry
- Protein Isoforms/genetics
- Protein Isoforms/metabolism
- Fish Proteins/chemistry*
- Fish Proteins/genetics
- Fish Proteins/metabolism
- Sequence Alignment
- Crystallography, X-Ray
- PubMed
- 24204770 Full text @ PLoS One
The avidin protein family members are well known for their high affinity towards D-biotin and high structural stability. These properties make avidins valuable tools for a wide range of biotechnology applications. We have identified a new member of the avidin family in the zebrafish (Danio rerio) genome, hereafter called zebavidin. The protein is highly expressed in the gonads of both male and female zebrafish and in the gills of male fish, but our data suggest that zebavidin is not crucial for the developing embryo. Biophysical and structural characterisation of zebavidin revealed distinct properties not found in any previously characterised avidins. Gel filtration chromatography and native mass spectrometry suggest that the protein forms dimers in the absence of biotin at low ionic strength, but assembles into tetramers upon binding biotin. Ligand binding was analysed using radioactive and fluorescently labelled biotin and isothermal titration calorimetry. Moreover, the crystal structure of zebavidin in complex with biotin was solved at 2.4 Å resolution and unveiled unique ligand binding and subunit interface architectures; the atomic-level details support our physicochemical observations.