Loading…

Zebavidin - An Avidin-Like Protein from Zebrafish: e77207

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) ge...

Full description

Saved in:
Bibliographic Details
Published in:PloS one 2013-10, Vol.8 (10)
Main Authors: Taskinen, Barbara, Zmurko, Joanna, Ojanen, Markus, Kukkurainen, Sampo, Parthiban, Marimuthu, Maeaettae, Juha AE, Leppiniemi, Jenni, Jaenis, Janne, Parikka, Mataleena, Turpeinen, Hannu
Format: Article
Language:English
Subjects:
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by
cites
container_end_page
container_issue 10
container_start_page
container_title PloS one
container_volume 8
creator Taskinen, Barbara
Zmurko, Joanna
Ojanen, Markus
Kukkurainen, Sampo
Parthiban, Marimuthu
Maeaettae, Juha AE
Leppiniemi, Jenni
Jaenis, Janne
Parikka, Mataleena
Turpeinen, Hannu
description 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.
doi_str_mv 10.1371/journal.pone.0077207
format article
fullrecord <record><control><sourceid>proquest</sourceid><recordid>TN_cdi_proquest_miscellaneous_1668265312</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>1668265312</sourcerecordid><originalsourceid>FETCH-proquest_miscellaneous_16682653123</originalsourceid><addsrcrecordid>eNqVjLsKwjAYRoMgWC9v4JDRpTUXmrRuRRQHBwcnlxL1L6amSU1an98ivoDTd-AcPoSWlCSUS7quXe-tMknrLCSESMmIHKGI5pzFghE-QdMQakJSngkRofwCV_XWd21xjAuLiy_HR_0EfPKug0FU3jV46LyqdHhsMHxP52hcKRNg8dsZWu135-0hbr179RC6stHhBsYoC64PJRUiYyLllPE_0g_N3T_k</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1668265312</pqid></control><display><type>article</type><title>Zebavidin - An Avidin-Like Protein from Zebrafish: e77207</title><source>Publicly Available Content Database (Proquest) (PQ_SDU_P3)</source><source>NCBI_PubMed Central(免费)</source><creator>Taskinen, Barbara ; Zmurko, Joanna ; Ojanen, Markus ; Kukkurainen, Sampo ; Parthiban, Marimuthu ; Maeaettae, Juha AE ; Leppiniemi, Jenni ; Jaenis, Janne ; Parikka, Mataleena ; Turpeinen, Hannu</creator><creatorcontrib>Taskinen, Barbara ; Zmurko, Joanna ; Ojanen, Markus ; Kukkurainen, Sampo ; Parthiban, Marimuthu ; Maeaettae, Juha AE ; Leppiniemi, Jenni ; Jaenis, Janne ; Parikka, Mataleena ; Turpeinen, Hannu</creatorcontrib><description>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.</description><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0077207</identifier><language>eng</language><subject>Danio rerio</subject><ispartof>PloS one, 2013-10, Vol.8 (10)</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925,37013</link.rule.ids></links><search><creatorcontrib>Taskinen, Barbara</creatorcontrib><creatorcontrib>Zmurko, Joanna</creatorcontrib><creatorcontrib>Ojanen, Markus</creatorcontrib><creatorcontrib>Kukkurainen, Sampo</creatorcontrib><creatorcontrib>Parthiban, Marimuthu</creatorcontrib><creatorcontrib>Maeaettae, Juha AE</creatorcontrib><creatorcontrib>Leppiniemi, Jenni</creatorcontrib><creatorcontrib>Jaenis, Janne</creatorcontrib><creatorcontrib>Parikka, Mataleena</creatorcontrib><creatorcontrib>Turpeinen, Hannu</creatorcontrib><title>Zebavidin - An Avidin-Like Protein from Zebrafish: e77207</title><title>PloS one</title><description>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.</description><subject>Danio rerio</subject><issn>1932-6203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><recordid>eNqVjLsKwjAYRoMgWC9v4JDRpTUXmrRuRRQHBwcnlxL1L6amSU1an98ivoDTd-AcPoSWlCSUS7quXe-tMknrLCSESMmIHKGI5pzFghE-QdMQakJSngkRofwCV_XWd21xjAuLiy_HR_0EfPKug0FU3jV46LyqdHhsMHxP52hcKRNg8dsZWu135-0hbr179RC6stHhBsYoC64PJRUiYyLllPE_0g_N3T_k</recordid><startdate>20131001</startdate><enddate>20131001</enddate><creator>Taskinen, Barbara</creator><creator>Zmurko, Joanna</creator><creator>Ojanen, Markus</creator><creator>Kukkurainen, Sampo</creator><creator>Parthiban, Marimuthu</creator><creator>Maeaettae, Juha AE</creator><creator>Leppiniemi, Jenni</creator><creator>Jaenis, Janne</creator><creator>Parikka, Mataleena</creator><creator>Turpeinen, Hannu</creator><scope>F1W</scope><scope>H95</scope><scope>L.G</scope></search><sort><creationdate>20131001</creationdate><title>Zebavidin - An Avidin-Like Protein from Zebrafish: e77207</title><author>Taskinen, Barbara ; Zmurko, Joanna ; Ojanen, Markus ; Kukkurainen, Sampo ; Parthiban, Marimuthu ; Maeaettae, Juha AE ; Leppiniemi, Jenni ; Jaenis, Janne ; Parikka, Mataleena ; Turpeinen, Hannu</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-proquest_miscellaneous_16682653123</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Danio rerio</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Taskinen, Barbara</creatorcontrib><creatorcontrib>Zmurko, Joanna</creatorcontrib><creatorcontrib>Ojanen, Markus</creatorcontrib><creatorcontrib>Kukkurainen, Sampo</creatorcontrib><creatorcontrib>Parthiban, Marimuthu</creatorcontrib><creatorcontrib>Maeaettae, Juha AE</creatorcontrib><creatorcontrib>Leppiniemi, Jenni</creatorcontrib><creatorcontrib>Jaenis, Janne</creatorcontrib><creatorcontrib>Parikka, Mataleena</creatorcontrib><creatorcontrib>Turpeinen, Hannu</creatorcontrib><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Aquatic Science &amp; Fisheries Abstracts (ASFA) 1: Biological Sciences &amp; Living Resources</collection><collection>Aquatic Science &amp; Fisheries Abstracts (ASFA) Professional</collection><jtitle>PloS one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Taskinen, Barbara</au><au>Zmurko, Joanna</au><au>Ojanen, Markus</au><au>Kukkurainen, Sampo</au><au>Parthiban, Marimuthu</au><au>Maeaettae, Juha AE</au><au>Leppiniemi, Jenni</au><au>Jaenis, Janne</au><au>Parikka, Mataleena</au><au>Turpeinen, Hannu</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Zebavidin - An Avidin-Like Protein from Zebrafish: e77207</atitle><jtitle>PloS one</jtitle><date>2013-10-01</date><risdate>2013</risdate><volume>8</volume><issue>10</issue><eissn>1932-6203</eissn><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.</abstract><doi>10.1371/journal.pone.0077207</doi></addata></record>
fulltext fulltext
identifier EISSN: 1932-6203
ispartof PloS one, 2013-10, Vol.8 (10)
issn 1932-6203
language eng
recordid cdi_proquest_miscellaneous_1668265312
source Publicly Available Content Database (Proquest) (PQ_SDU_P3); NCBI_PubMed Central(免费)
subjects Danio rerio
title Zebavidin - An Avidin-Like Protein from Zebrafish: e77207
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-30T01%3A13%3A12IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Zebavidin%20-%20An%20Avidin-Like%20Protein%20from%20Zebrafish:%20e77207&rft.jtitle=PloS%20one&rft.au=Taskinen,%20Barbara&rft.date=2013-10-01&rft.volume=8&rft.issue=10&rft.eissn=1932-6203&rft_id=info:doi/10.1371/journal.pone.0077207&rft_dat=%3Cproquest%3E1668265312%3C/proquest%3E%3Cgrp_id%3Ecdi_FETCH-proquest_miscellaneous_16682653123%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=1668265312&rft_id=info:pmid/&rfr_iscdi=true