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...
Saved in:
Published in: | PloS one 2013-10, Vol.8 (10) |
---|---|
Main Authors: | , , , , , , , , , |
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 & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>Aquatic Science & 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 |