A Major Latex-Like Protein Is a Key Factor in Crop Contamination by Persistent Organic Pollutants

This is the first report, to our knowledge, to reveal important factors by which members of the Cucurbitaceae family, such as cucumber (Cucumis sativus), watermelon (dtrullus lanatus), melon (Cucumis meld), pumpkin (Cucurbita pepo), squash (C. pepo), zucchini (C. pepo), are selectively polluted with...

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Veröffentlicht in:Plant physiology (Bethesda) 2013-04, Vol.161 (4), p.2128-2135
Hauptverfasser: Inui, Hideyuki, Sawada, Mami, Goto, Junya, Yamazaki, Kiyoshi, Kodama, Noriko, Tsuruta, Hiroki, Eun, Heesoo
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container_issue 4
container_start_page 2128
container_title Plant physiology (Bethesda)
container_volume 161
creator Inui, Hideyuki
Sawada, Mami
Goto, Junya
Yamazaki, Kiyoshi
Kodama, Noriko
Tsuruta, Hiroki
Eun, Heesoo
description This is the first report, to our knowledge, to reveal important factors by which members of the Cucurbitaceae family, such as cucumber (Cucumis sativus), watermelon (dtrullus lanatus), melon (Cucumis meld), pumpkin (Cucurbita pepo), squash (C. pepo), zucchini (C. pepo), are selectively polluted with highly toxic hydrophobic contaminants, including organochlorine insecticides and dioxins. Xylem sap of C. pepo ssp. pepo, which is a high accumulator of hydrophobic compounds, solubilized the hydrophobic compound pyrene into the aqueous phase via some protein(s). Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of xylem sap of two C. pepo subspecies revealed that the amount of 17-kD proteins in C. pepo ssp. pepo was larger than that in C. pepo ssp. ovifera, a low accumulator, suggesting that these proteins may be related to the translocation of hydrophobic compounds. The protein bands at 17 kD contained major latex-like proteins (MLPs), and the corresponding genes MLP-PG1, MLP-GR1, and MLP-GR3 were cloned from the C. pepo cultivars Patty Green and Gold Rush. Expression of the MLP-GR3 gene in C. pepo cultivars was positively correlated with the band intensity of 17-kD proteins and bioconcentration factors toward dioxins and dioxin-like compounds. Recombinant MLP-GR3 bound polychlorinated biphenyls immobilized on magnetic beads, whereas recombinant MLP-PG1 and MLP-GR1 did not. These results indicate that the high expression of MLP-GR3 in C. pepo ssp. pepo plants and the existence of MLP-GR3 in their xylem sap are related to the efficient translocation of hydrophobic contaminants. These findings should be useful for decreasing the contamination of fruit of the Cucurbitaceae family as well as the phytoremediation of hydrophobic contaminants.
doi_str_mv 10.1104/pp.112.213645
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Xylem sap of C. pepo ssp. pepo, which is a high accumulator of hydrophobic compounds, solubilized the hydrophobic compound pyrene into the aqueous phase via some protein(s). Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of xylem sap of two C. pepo subspecies revealed that the amount of 17-kD proteins in C. pepo ssp. pepo was larger than that in C. pepo ssp. ovifera, a low accumulator, suggesting that these proteins may be related to the translocation of hydrophobic compounds. The protein bands at 17 kD contained major latex-like proteins (MLPs), and the corresponding genes MLP-PG1, MLP-GR1, and MLP-GR3 were cloned from the C. pepo cultivars Patty Green and Gold Rush. Expression of the MLP-GR3 gene in C. pepo cultivars was positively correlated with the band intensity of 17-kD proteins and bioconcentration factors toward dioxins and dioxin-like compounds. Recombinant MLP-GR3 bound polychlorinated biphenyls immobilized on magnetic beads, whereas recombinant MLP-PG1 and MLP-GR1 did not. These results indicate that the high expression of MLP-GR3 in C. pepo ssp. pepo plants and the existence of MLP-GR3 in their xylem sap are related to the efficient translocation of hydrophobic contaminants. These findings should be useful for decreasing the contamination of fruit of the Cucurbitaceae family as well as the phytoremediation of hydrophobic contaminants.</description><identifier>ISSN: 0032-0889</identifier><identifier>ISSN: 1532-2548</identifier><identifier>EISSN: 1532-2548</identifier><identifier>DOI: 10.1104/pp.112.213645</identifier><identifier>PMID: 23404917</identifier><identifier>CODEN: PPHYA5</identifier><language>eng</language><publisher>Rockville, MD: American Society of Plant Biologists</publisher><subject>Aerial parts ; Amino Acid Sequence ; Amino acids ; Biological and medical sciences ; Cloning, Molecular ; Crops, Agricultural - metabolism ; Cucumbers ; Cucurbita - genetics ; Cucurbita - metabolism ; Dioxins ; Electrophoresis, Polyacrylamide Gel ; Fundamental and applied biological sciences. Psychology ; Gene Expression Regulation, Plant ; Genes, Plant - genetics ; Latex - metabolism ; MEMBRANES, TRANSPORT, AND BIOENERGETICS ; Molecular Sequence Data ; Organic Chemicals - metabolism ; Pepos ; Persistent organic pollutants ; Plant physiology and development ; Plant Proteins - chemistry ; Plant Proteins - metabolism ; Plant Roots - genetics ; Plants ; Polychlorinated Biphenyls - metabolism ; Protein Binding ; Proteins ; Pyrenes - metabolism ; Recombinant Proteins - metabolism ; Sequence Alignment ; Soil Pollutants - metabolism ; Solubility ; Solubilization ; Xylem ; Xylem - metabolism</subject><ispartof>Plant physiology (Bethesda), 2013-04, Vol.161 (4), p.2128-2135</ispartof><rights>2013 American Society of Plant Biologists</rights><rights>2014 INIST-CNRS</rights><rights>2013 American Society of Plant Biologists. 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Xylem sap of C. pepo ssp. pepo, which is a high accumulator of hydrophobic compounds, solubilized the hydrophobic compound pyrene into the aqueous phase via some protein(s). Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of xylem sap of two C. pepo subspecies revealed that the amount of 17-kD proteins in C. pepo ssp. pepo was larger than that in C. pepo ssp. ovifera, a low accumulator, suggesting that these proteins may be related to the translocation of hydrophobic compounds. The protein bands at 17 kD contained major latex-like proteins (MLPs), and the corresponding genes MLP-PG1, MLP-GR1, and MLP-GR3 were cloned from the C. pepo cultivars Patty Green and Gold Rush. Expression of the MLP-GR3 gene in C. pepo cultivars was positively correlated with the band intensity of 17-kD proteins and bioconcentration factors toward dioxins and dioxin-like compounds. Recombinant MLP-GR3 bound polychlorinated biphenyls immobilized on magnetic beads, whereas recombinant MLP-PG1 and MLP-GR1 did not. These results indicate that the high expression of MLP-GR3 in C. pepo ssp. pepo plants and the existence of MLP-GR3 in their xylem sap are related to the efficient translocation of hydrophobic contaminants. These findings should be useful for decreasing the contamination of fruit of the Cucurbitaceae family as well as the phytoremediation of hydrophobic contaminants.</description><subject>Aerial parts</subject><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Biological and medical sciences</subject><subject>Cloning, Molecular</subject><subject>Crops, Agricultural - metabolism</subject><subject>Cucumbers</subject><subject>Cucurbita - genetics</subject><subject>Cucurbita - metabolism</subject><subject>Dioxins</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Expression Regulation, Plant</subject><subject>Genes, Plant - genetics</subject><subject>Latex - metabolism</subject><subject>MEMBRANES, TRANSPORT, AND BIOENERGETICS</subject><subject>Molecular Sequence Data</subject><subject>Organic Chemicals - metabolism</subject><subject>Pepos</subject><subject>Persistent organic pollutants</subject><subject>Plant physiology and development</subject><subject>Plant Proteins - chemistry</subject><subject>Plant Proteins - metabolism</subject><subject>Plant Roots - genetics</subject><subject>Plants</subject><subject>Polychlorinated Biphenyls - metabolism</subject><subject>Protein Binding</subject><subject>Proteins</subject><subject>Pyrenes - metabolism</subject><subject>Recombinant Proteins - metabolism</subject><subject>Sequence Alignment</subject><subject>Soil Pollutants - metabolism</subject><subject>Solubility</subject><subject>Solubilization</subject><subject>Xylem</subject><subject>Xylem - metabolism</subject><issn>0032-0889</issn><issn>1532-2548</issn><issn>1532-2548</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkEFPGzEQhS1UBIH22GMrXzgu2GNv1nuphCJSUIPIoT2vZr3e1OnGXtkOIv8el9AUTm80882b0SPkM2eXnDN5NY5Z4RK4mMryiEx4KaCAUqoPZMJYrplS9Sk5i3HNGOOCyxNyCkIyWfNqQvCa3uPaB7rAZJ6Khf1j6DL4ZKyjd5Ei_WF2dI46ZSS3ZsGPdOZdwo11mKx3tN3RpQnRxmRcog9hhc5quvTDsE3oUvxIjnscovn0qufk1_zm5-y2WDx8v5tdLwpdsjIVtelapkG2wghdAhimelEp0xkNrKy4gL5C0L0ooeKtqmVnaiEQseprqTotzsm3ve-4bTem0_mbgEMzBrvBsGs82ub9xNnfzco_NmLKhVQ8GxR7Ax18jMH0h13Omr9ZN-OYFZp91pn_-vbggf4XbgYuXgGMGoc-oNM2_ucqAMZfuC97bh1zzIe55LUEJUA8AzwBkec</recordid><startdate>20130401</startdate><enddate>20130401</enddate><creator>Inui, Hideyuki</creator><creator>Sawada, Mami</creator><creator>Goto, Junya</creator><creator>Yamazaki, Kiyoshi</creator><creator>Kodama, Noriko</creator><creator>Tsuruta, Hiroki</creator><creator>Eun, Heesoo</creator><general>American Society of Plant Biologists</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>5PM</scope></search><sort><creationdate>20130401</creationdate><title>A Major Latex-Like Protein Is a Key Factor in Crop Contamination by Persistent Organic Pollutants</title><author>Inui, Hideyuki ; Sawada, Mami ; Goto, Junya ; Yamazaki, Kiyoshi ; Kodama, Noriko ; Tsuruta, Hiroki ; Eun, Heesoo</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c505t-9edb0c24b3e3c522e08f378edec2057132f7a2cf35271b894de933aaa7f948dc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Aerial parts</topic><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Biological and medical sciences</topic><topic>Cloning, Molecular</topic><topic>Crops, Agricultural - metabolism</topic><topic>Cucumbers</topic><topic>Cucurbita - genetics</topic><topic>Cucurbita - metabolism</topic><topic>Dioxins</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene Expression Regulation, Plant</topic><topic>Genes, Plant - genetics</topic><topic>Latex - metabolism</topic><topic>MEMBRANES, TRANSPORT, AND BIOENERGETICS</topic><topic>Molecular Sequence Data</topic><topic>Organic Chemicals - metabolism</topic><topic>Pepos</topic><topic>Persistent organic pollutants</topic><topic>Plant physiology and development</topic><topic>Plant Proteins - chemistry</topic><topic>Plant Proteins - metabolism</topic><topic>Plant Roots - genetics</topic><topic>Plants</topic><topic>Polychlorinated Biphenyls - metabolism</topic><topic>Protein Binding</topic><topic>Proteins</topic><topic>Pyrenes - metabolism</topic><topic>Recombinant Proteins - metabolism</topic><topic>Sequence Alignment</topic><topic>Soil Pollutants - metabolism</topic><topic>Solubility</topic><topic>Solubilization</topic><topic>Xylem</topic><topic>Xylem - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Inui, Hideyuki</creatorcontrib><creatorcontrib>Sawada, Mami</creatorcontrib><creatorcontrib>Goto, Junya</creatorcontrib><creatorcontrib>Yamazaki, Kiyoshi</creatorcontrib><creatorcontrib>Kodama, Noriko</creatorcontrib><creatorcontrib>Tsuruta, Hiroki</creatorcontrib><creatorcontrib>Eun, Heesoo</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Plant physiology (Bethesda)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Inui, Hideyuki</au><au>Sawada, Mami</au><au>Goto, Junya</au><au>Yamazaki, Kiyoshi</au><au>Kodama, Noriko</au><au>Tsuruta, Hiroki</au><au>Eun, Heesoo</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A Major Latex-Like Protein Is a Key Factor in Crop Contamination by Persistent Organic Pollutants</atitle><jtitle>Plant physiology (Bethesda)</jtitle><addtitle>Plant Physiol</addtitle><date>2013-04-01</date><risdate>2013</risdate><volume>161</volume><issue>4</issue><spage>2128</spage><epage>2135</epage><pages>2128-2135</pages><issn>0032-0889</issn><issn>1532-2548</issn><eissn>1532-2548</eissn><coden>PPHYA5</coden><abstract>This is the first report, to our knowledge, to reveal important factors by which members of the Cucurbitaceae family, such as cucumber (Cucumis sativus), watermelon (dtrullus lanatus), melon (Cucumis meld), pumpkin (Cucurbita pepo), squash (C. pepo), zucchini (C. pepo), are selectively polluted with highly toxic hydrophobic contaminants, including organochlorine insecticides and dioxins. Xylem sap of C. pepo ssp. pepo, which is a high accumulator of hydrophobic compounds, solubilized the hydrophobic compound pyrene into the aqueous phase via some protein(s). Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of xylem sap of two C. pepo subspecies revealed that the amount of 17-kD proteins in C. pepo ssp. pepo was larger than that in C. pepo ssp. ovifera, a low accumulator, suggesting that these proteins may be related to the translocation of hydrophobic compounds. The protein bands at 17 kD contained major latex-like proteins (MLPs), and the corresponding genes MLP-PG1, MLP-GR1, and MLP-GR3 were cloned from the C. pepo cultivars Patty Green and Gold Rush. Expression of the MLP-GR3 gene in C. pepo cultivars was positively correlated with the band intensity of 17-kD proteins and bioconcentration factors toward dioxins and dioxin-like compounds. Recombinant MLP-GR3 bound polychlorinated biphenyls immobilized on magnetic beads, whereas recombinant MLP-PG1 and MLP-GR1 did not. These results indicate that the high expression of MLP-GR3 in C. pepo ssp. pepo plants and the existence of MLP-GR3 in their xylem sap are related to the efficient translocation of hydrophobic contaminants. These findings should be useful for decreasing the contamination of fruit of the Cucurbitaceae family as well as the phytoremediation of hydrophobic contaminants.</abstract><cop>Rockville, MD</cop><pub>American Society of Plant Biologists</pub><pmid>23404917</pmid><doi>10.1104/pp.112.213645</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record>
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subjects Aerial parts
Amino Acid Sequence
Amino acids
Biological and medical sciences
Cloning, Molecular
Crops, Agricultural - metabolism
Cucumbers
Cucurbita - genetics
Cucurbita - metabolism
Dioxins
Electrophoresis, Polyacrylamide Gel
Fundamental and applied biological sciences. Psychology
Gene Expression Regulation, Plant
Genes, Plant - genetics
Latex - metabolism
MEMBRANES, TRANSPORT, AND BIOENERGETICS
Molecular Sequence Data
Organic Chemicals - metabolism
Pepos
Persistent organic pollutants
Plant physiology and development
Plant Proteins - chemistry
Plant Proteins - metabolism
Plant Roots - genetics
Plants
Polychlorinated Biphenyls - metabolism
Protein Binding
Proteins
Pyrenes - metabolism
Recombinant Proteins - metabolism
Sequence Alignment
Soil Pollutants - metabolism
Solubility
Solubilization
Xylem
Xylem - metabolism
title A Major Latex-Like Protein Is a Key Factor in Crop Contamination by Persistent Organic Pollutants
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