Role of a Carboxylesterase in Herbicide Bioactivation in Arabidopsis thaliana
Arabidopsis thaliana contains multiple carboxyesterases (AtCXEs) with activities toward xenobiotics, including herbicide esters that are activated to their phytotoxic acids upon hydrolysis. On the basis of their susceptibility to inhibition by organophosphates, these AtCXEs are all serine hydrolases...
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Veröffentlicht in: | The Journal of biological chemistry 2007-07, Vol.282 (29), p.21460-21466 |
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description | Arabidopsis thaliana contains multiple carboxyesterases (AtCXEs) with activities toward xenobiotics, including herbicide esters that are activated to their phytotoxic acids upon hydrolysis. On the basis of their susceptibility to inhibition by organophosphates, these AtCXEs are all serine hydrolases. Using a trifunctional probe bearing a fluorophosphonate together with biotin and rhodamine to facilitate detection and recovery, four dominant serine hydrolases were identified in the proteome of Arabidopsis. Using a combination of protein purification, capture with the trifunctional probe and proteomics, one of these hydrolases, AtCXE12, was shown to be the major carboxyesterase responsible for hydrolyzing the pro-herbicide methyl-2,4-dichlorophenoxyacetate (2,4-D-methyl) to the phytotoxic acid 2,4-dichlorophenoxyacetic acid. Recombinant expression of the other identified hydrolases showed that AtCXE12 was unique in hydrolyzing 2,4-D-methyl. To determine the importance of AtCXE12 in herbicide metabolism and efficacy, the respective tDNA knock-out (atcxe12) plants were characterized and shown to lack expression of AtCXE12 and have greatly reduced levels of 2,4-D-methyl-hydrolyzing activity. Young atcxe12 seedlings were less sensitive than wild type plants to 2,4-D-methyl, confirming a role for the enzyme in herbicide bioactivation in Arabidopsis. |
doi_str_mv | 10.1074/jbc.M701985200 |
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On the basis of their susceptibility to inhibition by organophosphates, these AtCXEs are all serine hydrolases. Using a trifunctional probe bearing a fluorophosphonate together with biotin and rhodamine to facilitate detection and recovery, four dominant serine hydrolases were identified in the proteome of Arabidopsis. Using a combination of protein purification, capture with the trifunctional probe and proteomics, one of these hydrolases, AtCXE12, was shown to be the major carboxyesterase responsible for hydrolyzing the pro-herbicide methyl-2,4-dichlorophenoxyacetate (2,4-D-methyl) to the phytotoxic acid 2,4-dichlorophenoxyacetic acid. Recombinant expression of the other identified hydrolases showed that AtCXE12 was unique in hydrolyzing 2,4-D-methyl. To determine the importance of AtCXE12 in herbicide metabolism and efficacy, the respective tDNA knock-out (atcxe12) plants were characterized and shown to lack expression of AtCXE12 and have greatly reduced levels of 2,4-D-methyl-hydrolyzing activity. Young atcxe12 seedlings were less sensitive than wild type plants to 2,4-D-methyl, confirming a role for the enzyme in herbicide bioactivation in Arabidopsis.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M701985200</identifier><identifier>PMID: 17519238</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>2,4-Dichlorophenoxyacetic Acid - chemistry ; Arabidopsis - enzymology ; Carboxylesterase - chemistry ; Cloning, Molecular ; Gene Expression Regulation, Plant ; Herbicides - chemistry ; Hydrolases - chemistry ; Hydrolysis ; Models, Chemical ; Organophosphonates - chemistry ; Proteins - chemistry ; Seedlings ; Xenobiotics - chemistry</subject><ispartof>The Journal of biological chemistry, 2007-07, Vol.282 (29), p.21460-21466</ispartof><rights>2007 © 2007 ASBMB. 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On the basis of their susceptibility to inhibition by organophosphates, these AtCXEs are all serine hydrolases. Using a trifunctional probe bearing a fluorophosphonate together with biotin and rhodamine to facilitate detection and recovery, four dominant serine hydrolases were identified in the proteome of Arabidopsis. Using a combination of protein purification, capture with the trifunctional probe and proteomics, one of these hydrolases, AtCXE12, was shown to be the major carboxyesterase responsible for hydrolyzing the pro-herbicide methyl-2,4-dichlorophenoxyacetate (2,4-D-methyl) to the phytotoxic acid 2,4-dichlorophenoxyacetic acid. Recombinant expression of the other identified hydrolases showed that AtCXE12 was unique in hydrolyzing 2,4-D-methyl. To determine the importance of AtCXE12 in herbicide metabolism and efficacy, the respective tDNA knock-out (atcxe12) plants were characterized and shown to lack expression of AtCXE12 and have greatly reduced levels of 2,4-D-methyl-hydrolyzing activity. Young atcxe12 seedlings were less sensitive than wild type plants to 2,4-D-methyl, confirming a role for the enzyme in herbicide bioactivation in Arabidopsis.</description><subject>2,4-Dichlorophenoxyacetic Acid - chemistry</subject><subject>Arabidopsis - enzymology</subject><subject>Carboxylesterase - chemistry</subject><subject>Cloning, Molecular</subject><subject>Gene Expression Regulation, Plant</subject><subject>Herbicides - chemistry</subject><subject>Hydrolases - chemistry</subject><subject>Hydrolysis</subject><subject>Models, Chemical</subject><subject>Organophosphonates - chemistry</subject><subject>Proteins - chemistry</subject><subject>Seedlings</subject><subject>Xenobiotics - chemistry</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kD1PwzAQhi0EoqWwMqIMrCn-SuKMpQKKRIWEQGKzbOdMXKVxZYdC_z2pUqkTt9xwz3u6exC6JnhKcMHvVtpMlwUmpcgoxidoTLBgKcvI5ykaY0xJWtJMjNBFjCvcFy_JORqRIiMlZWKMlm--gcTbRCVzFbT_3TUQOwgqQuLaZAFBO-MqSO6dV6ZzW9U53-5Hs6C0q_wmuph0tWqcatUlOrOqiXB16BP08fjwPl-kL69Pz_PZS2p4UXSprVSOrS15njHghClbljmoQlijCGhjwQClBWWswLmi1gLloFmWW60Fz4BN0HTYa4KPMYCVm-DWKuwkwXLvRfZe5NFLH7gZAptvvYbqiB9E9MDtANTuq_5xAaR23tSwllRQSUtJCc_3e8SAQf_d1kGQ0ThoDVR9xHSy8u6_E_4A7Ul-Mg</recordid><startdate>20070720</startdate><enddate>20070720</enddate><creator>Gershater, Markus C.</creator><creator>Cummins, Ian</creator><creator>Edwards, Robert</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</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></search><sort><creationdate>20070720</creationdate><title>Role of a Carboxylesterase in Herbicide Bioactivation in Arabidopsis thaliana</title><author>Gershater, Markus C. ; Cummins, Ian ; Edwards, Robert</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c477t-fda60ff94653e413af996ea78fca1ebcfece227233706a2ffe24eb356fbb845e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>2,4-Dichlorophenoxyacetic Acid - chemistry</topic><topic>Arabidopsis - enzymology</topic><topic>Carboxylesterase - chemistry</topic><topic>Cloning, Molecular</topic><topic>Gene Expression Regulation, Plant</topic><topic>Herbicides - chemistry</topic><topic>Hydrolases - chemistry</topic><topic>Hydrolysis</topic><topic>Models, Chemical</topic><topic>Organophosphonates - chemistry</topic><topic>Proteins - chemistry</topic><topic>Seedlings</topic><topic>Xenobiotics - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gershater, Markus C.</creatorcontrib><creatorcontrib>Cummins, Ian</creatorcontrib><creatorcontrib>Edwards, Robert</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gershater, Markus C.</au><au>Cummins, Ian</au><au>Edwards, Robert</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Role of a Carboxylesterase in Herbicide Bioactivation in Arabidopsis thaliana</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2007-07-20</date><risdate>2007</risdate><volume>282</volume><issue>29</issue><spage>21460</spage><epage>21466</epage><pages>21460-21466</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Arabidopsis thaliana contains multiple carboxyesterases (AtCXEs) with activities toward xenobiotics, including herbicide esters that are activated to their phytotoxic acids upon hydrolysis. On the basis of their susceptibility to inhibition by organophosphates, these AtCXEs are all serine hydrolases. Using a trifunctional probe bearing a fluorophosphonate together with biotin and rhodamine to facilitate detection and recovery, four dominant serine hydrolases were identified in the proteome of Arabidopsis. Using a combination of protein purification, capture with the trifunctional probe and proteomics, one of these hydrolases, AtCXE12, was shown to be the major carboxyesterase responsible for hydrolyzing the pro-herbicide methyl-2,4-dichlorophenoxyacetate (2,4-D-methyl) to the phytotoxic acid 2,4-dichlorophenoxyacetic acid. Recombinant expression of the other identified hydrolases showed that AtCXE12 was unique in hydrolyzing 2,4-D-methyl. To determine the importance of AtCXE12 in herbicide metabolism and efficacy, the respective tDNA knock-out (atcxe12) plants were characterized and shown to lack expression of AtCXE12 and have greatly reduced levels of 2,4-D-methyl-hydrolyzing activity. Young atcxe12 seedlings were less sensitive than wild type plants to 2,4-D-methyl, confirming a role for the enzyme in herbicide bioactivation in Arabidopsis.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>17519238</pmid><doi>10.1074/jbc.M701985200</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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subjects | 2,4-Dichlorophenoxyacetic Acid - chemistry Arabidopsis - enzymology Carboxylesterase - chemistry Cloning, Molecular Gene Expression Regulation, Plant Herbicides - chemistry Hydrolases - chemistry Hydrolysis Models, Chemical Organophosphonates - chemistry Proteins - chemistry Seedlings Xenobiotics - chemistry |
title | Role of a Carboxylesterase in Herbicide Bioactivation in Arabidopsis thaliana |
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