Zebavidin - An Avidin-Like Protein from Zebrafish

Barbara Taskinen, Joanna Zmurko, Markus Ojanen, Sampo Kukkurainen, Marimuthu Parthiban, Juha A E Määttä, Jenni Leppiniemi, Janne Jänis, Mataleena Parikka, Hannu Turpeinen, Mika Rämet, Marko Pesu, Mark S. Johnson, Markku S. Kulomaa, Tomi T. Airenne, Vesa P. Hytönen

Tutkimustuotos: ArtikkeliScientificvertaisarvioitu

14 Sitaatiot (Scopus)

Abstrakti

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.

AlkuperäiskieliEnglanti
Artikkelie77207
Sivute77207
JulkaisuPLOS One
Vuosikerta8
Numero10
DOI - pysyväislinkit
TilaJulkaistu - 2013
OKM-julkaisutyyppiA1 Alkuperäisartikkeli tieteellisessä aikakauslehdessä

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