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Zebavidin - An Avidin-Like Protein from Zebrafish

Tutkimustuotosvertaisarvioitu

Standard

Zebavidin - An Avidin-Like Protein from Zebrafish. / Taskinen, Barbara; Zmurko, Joanna; Ojanen, Markus; Kukkurainen, Sampo; Parthiban, Marimuthu; Määttä, Juha A E; Leppiniemi, Jenni; Jänis, Janne; Parikka, Mataleena; Turpeinen, Hannu; Rämet, Mika; Pesu, Marko; Johnson, Mark S.; Kulomaa, Markku S.; Airenne, Tomi T.; Hytönen, Vesa P.

julkaisussa: PLoS ONE, Vuosikerta 8, Nro 10, e77207, 24.10.2013.

Tutkimustuotosvertaisarvioitu

Harvard

Taskinen, B, Zmurko, J, Ojanen, M, Kukkurainen, S, Parthiban, M, Määttä, JAE, Leppiniemi, J, Jänis, J, Parikka, M, Turpeinen, H, Rämet, M, Pesu, M, Johnson, MS, Kulomaa, MS, Airenne, TT & Hytönen, VP 2013, 'Zebavidin - An Avidin-Like Protein from Zebrafish', PLoS ONE, Vuosikerta. 8, Nro 10, e77207. https://doi.org/10.1371/journal.pone.0077207

APA

Taskinen, B., Zmurko, J., Ojanen, M., Kukkurainen, S., Parthiban, M., Määttä, J. A. E., ... Hytönen, V. P. (2013). Zebavidin - An Avidin-Like Protein from Zebrafish. PLoS ONE, 8(10), [e77207]. https://doi.org/10.1371/journal.pone.0077207

Vancouver

Taskinen B, Zmurko J, Ojanen M, Kukkurainen S, Parthiban M, Määttä JAE et al. Zebavidin - An Avidin-Like Protein from Zebrafish. PLoS ONE. 2013 loka 24;8(10). e77207. https://doi.org/10.1371/journal.pone.0077207

Author

Taskinen, Barbara ; Zmurko, Joanna ; Ojanen, Markus ; Kukkurainen, Sampo ; Parthiban, Marimuthu ; Määttä, Juha A E ; Leppiniemi, Jenni ; Jänis, Janne ; Parikka, Mataleena ; Turpeinen, Hannu ; Rämet, Mika ; Pesu, Marko ; Johnson, Mark S. ; Kulomaa, Markku S. ; Airenne, Tomi T. ; Hytönen, Vesa P. / Zebavidin - An Avidin-Like Protein from Zebrafish. Julkaisussa: PLoS ONE. 2013 ; Vuosikerta 8, Nro 10.

Bibtex - Lataa

@article{0411826b810d44ebb84702cf94650d90,
title = "Zebavidin - An Avidin-Like Protein from Zebrafish",
abstract = "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 {\AA} resolution and unveiled unique ligand binding and subunit interface architectures; the atomic-level details support our physicochemical observations.",
author = "Barbara Taskinen and Joanna Zmurko and Markus Ojanen and Sampo Kukkurainen and Marimuthu Parthiban and M{\"a}{\"a}tt{\"a}, {Juha A E} and Jenni Leppiniemi and Janne J{\"a}nis and Mataleena Parikka and Hannu Turpeinen and Mika R{\"a}met and Marko Pesu and Johnson, {Mark S.} and Kulomaa, {Markku S.} and Airenne, {Tomi T.} and Hyt{\"o}nen, {Vesa P.}",
year = "2013",
month = "10",
day = "24",
doi = "10.1371/journal.pone.0077207",
language = "English",
volume = "8",
journal = "PLoS ONE",
issn = "1932-6203",
publisher = "Public Library of Science",
number = "10",

}

RIS (suitable for import to EndNote) - Lataa

TY - JOUR

T1 - Zebavidin - An Avidin-Like Protein from Zebrafish

AU - Taskinen, Barbara

AU - Zmurko, Joanna

AU - Ojanen, Markus

AU - Kukkurainen, Sampo

AU - Parthiban, Marimuthu

AU - Määttä, Juha A E

AU - Leppiniemi, Jenni

AU - Jänis, Janne

AU - Parikka, Mataleena

AU - Turpeinen, Hannu

AU - Rämet, Mika

AU - Pesu, Marko

AU - Johnson, Mark S.

AU - Kulomaa, Markku S.

AU - Airenne, Tomi T.

AU - Hytönen, Vesa P.

PY - 2013/10/24

Y1 - 2013/10/24

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=84886258385&partnerID=8YFLogxK

U2 - 10.1371/journal.pone.0077207

DO - 10.1371/journal.pone.0077207

M3 - Article

VL - 8

JO - PLoS ONE

JF - PLoS ONE

SN - 1932-6203

IS - 10

M1 - e77207

ER -