Cysteine proteases are activated in sensitive Amaranthus palmeri populations upon treatment with herbicides inhibiting amino acid biosynthesis
The herbicides glyphosate and pyrithiobac inhibit the enzyme 5‐enolpyruvylshikimate‐3‐phosphate synthase (EPSPS) in the aromatic amino acid biosynthetic pathway and acetolactate synthase (ALS) in the branched‐chain amino acid biosynthetic pathway, respectively. Here we characterise the protease acti...
Gespeichert in:
| Veröffentlicht in: | Physiologia plantarum 2023-09, Vol.175 (5), p.e13993-n/a |
|---|---|
| Hauptverfasser: | , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | n/a |
|---|---|
| container_issue | 5 |
| container_start_page | e13993 |
| container_title | Physiologia plantarum |
| container_volume | 175 |
| creator | Barco‐Antoñanzas, Maria Font‐Farre, Maria Eceiza, Mikel V. Gil‐Monreal, Miriam van der Hoorn, Renier A. L. Royuela, Mercedes Zabalza, Ana |
| description | The herbicides glyphosate and pyrithiobac inhibit the enzyme 5‐enolpyruvylshikimate‐3‐phosphate synthase (EPSPS) in the aromatic amino acid biosynthetic pathway and acetolactate synthase (ALS) in the branched‐chain amino acid biosynthetic pathway, respectively. Here we characterise the protease activity profiles of a sensitive (S), a glyphosate‐resistant (GR) and a multiple‐resistant (MR) population of Amaranthus palmeri in response to glyphosate and pyrithiobac. Amino acid accumulation and cysteine protease activities were induced with both herbicides in the S population and with pyrithiobac in the GR population, suggesting that the increase in cysteine proteases is responsible for the increased degradation of the available proteins and the observed increase in free amino acids. Herbicides did not induce any changes in the proteolytic activities in the populations with target‐site resistance, indicating that this effect was only induced in sensitive plants. |
| doi_str_mv | 10.1111/ppl.13993 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_2882324550</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2882324550</sourcerecordid><originalsourceid>FETCH-LOGICAL-c3653-ba667a131137553b8182544f9d84e947dc4d7d6fbbe4a925514f1ecd3ac0012d3</originalsourceid><addsrcrecordid>eNp1kU1r3DAQhkVJoZttD_0Hgl7agxPJkvxxDEvSFhaSQ3s2sjXuTrAlVyMn7J_ob46221MhcxkGnnnn42XsoxRXMsf1skxXUrWtesM2p1woYfQF2wihZNEqWb9jl0SPQsiqkuWG_dkdKQF64EsMCSwBcRuB2yHhk03gOHpO4AlzDfxmttH6dFiJL3aaISJfwrJONmHwxNcleJ4i2DSDT_wZ04EfIPY4oMvC6A_YZyH_i9sZfchT0PEeAx2zJhDSe_Z2tBPBh395y37e3f7YfSv291-_7272xaAqo4reVlVtpZJS1caovpFNabQeW9doaHXtBu1qV419D9q2pTFSjxIGp-yQLy-d2rLPZ9189e8VKHUz0gDTZD2ElbqyaUpVamNERj_9hz6GNfq83YmSlRa6bjL15UwNMRBFGLslYn7WsZOiOznTZWe6v85k9vrMPuMEx9fB7uFhf-54AWt6kyQ</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2881640478</pqid></control><display><type>article</type><title>Cysteine proteases are activated in sensitive Amaranthus palmeri populations upon treatment with herbicides inhibiting amino acid biosynthesis</title><source>Wiley Online Library All Journals</source><creator>Barco‐Antoñanzas, Maria ; Font‐Farre, Maria ; Eceiza, Mikel V. ; Gil‐Monreal, Miriam ; van der Hoorn, Renier A. L. ; Royuela, Mercedes ; Zabalza, Ana</creator><creatorcontrib>Barco‐Antoñanzas, Maria ; Font‐Farre, Maria ; Eceiza, Mikel V. ; Gil‐Monreal, Miriam ; van der Hoorn, Renier A. L. ; Royuela, Mercedes ; Zabalza, Ana</creatorcontrib><description>The herbicides glyphosate and pyrithiobac inhibit the enzyme 5‐enolpyruvylshikimate‐3‐phosphate synthase (EPSPS) in the aromatic amino acid biosynthetic pathway and acetolactate synthase (ALS) in the branched‐chain amino acid biosynthetic pathway, respectively. Here we characterise the protease activity profiles of a sensitive (S), a glyphosate‐resistant (GR) and a multiple‐resistant (MR) population of Amaranthus palmeri in response to glyphosate and pyrithiobac. Amino acid accumulation and cysteine protease activities were induced with both herbicides in the S population and with pyrithiobac in the GR population, suggesting that the increase in cysteine proteases is responsible for the increased degradation of the available proteins and the observed increase in free amino acids. Herbicides did not induce any changes in the proteolytic activities in the populations with target‐site resistance, indicating that this effect was only induced in sensitive plants.</description><identifier>ISSN: 0031-9317</identifier><identifier>EISSN: 1399-3054</identifier><identifier>DOI: 10.1111/ppl.13993</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Acetolactate synthase ; Amaranthus palmeri ; Amino acids ; Biosynthesis ; Chain branching ; Cysteine ; Cysteine proteinase ; Glyphosate ; Herbicides ; Populations ; Protease ; Proteolysis</subject><ispartof>Physiologia plantarum, 2023-09, Vol.175 (5), p.e13993-n/a</ispartof><rights>2023 The Authors. published by John Wiley & Sons Ltd on behalf of Scandinavian Plant Physiology Society.</rights><rights>2023. This article is published under http://creativecommons.org/licenses/by-nc-nd/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3653-ba667a131137553b8182544f9d84e947dc4d7d6fbbe4a925514f1ecd3ac0012d3</citedby><cites>FETCH-LOGICAL-c3653-ba667a131137553b8182544f9d84e947dc4d7d6fbbe4a925514f1ecd3ac0012d3</cites><orcidid>0000-0002-4086-9590 ; 0000-0003-4554-6798 ; 0000-0002-1085-2229 ; 0000-0002-6622-2234 ; 0000-0002-1684-270X ; 0000-0002-3692-7487 ; 0000-0001-6954-6317</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fppl.13993$$EPDF$$P50$$Gwiley$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fppl.13993$$EHTML$$P50$$Gwiley$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,1411,27901,27902,45550,45551</link.rule.ids></links><search><creatorcontrib>Barco‐Antoñanzas, Maria</creatorcontrib><creatorcontrib>Font‐Farre, Maria</creatorcontrib><creatorcontrib>Eceiza, Mikel V.</creatorcontrib><creatorcontrib>Gil‐Monreal, Miriam</creatorcontrib><creatorcontrib>van der Hoorn, Renier A. L.</creatorcontrib><creatorcontrib>Royuela, Mercedes</creatorcontrib><creatorcontrib>Zabalza, Ana</creatorcontrib><title>Cysteine proteases are activated in sensitive Amaranthus palmeri populations upon treatment with herbicides inhibiting amino acid biosynthesis</title><title>Physiologia plantarum</title><description>The herbicides glyphosate and pyrithiobac inhibit the enzyme 5‐enolpyruvylshikimate‐3‐phosphate synthase (EPSPS) in the aromatic amino acid biosynthetic pathway and acetolactate synthase (ALS) in the branched‐chain amino acid biosynthetic pathway, respectively. Here we characterise the protease activity profiles of a sensitive (S), a glyphosate‐resistant (GR) and a multiple‐resistant (MR) population of Amaranthus palmeri in response to glyphosate and pyrithiobac. Amino acid accumulation and cysteine protease activities were induced with both herbicides in the S population and with pyrithiobac in the GR population, suggesting that the increase in cysteine proteases is responsible for the increased degradation of the available proteins and the observed increase in free amino acids. Herbicides did not induce any changes in the proteolytic activities in the populations with target‐site resistance, indicating that this effect was only induced in sensitive plants.</description><subject>Acetolactate synthase</subject><subject>Amaranthus palmeri</subject><subject>Amino acids</subject><subject>Biosynthesis</subject><subject>Chain branching</subject><subject>Cysteine</subject><subject>Cysteine proteinase</subject><subject>Glyphosate</subject><subject>Herbicides</subject><subject>Populations</subject><subject>Protease</subject><subject>Proteolysis</subject><issn>0031-9317</issn><issn>1399-3054</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><sourceid>24P</sourceid><recordid>eNp1kU1r3DAQhkVJoZttD_0Hgl7agxPJkvxxDEvSFhaSQ3s2sjXuTrAlVyMn7J_ob46221MhcxkGnnnn42XsoxRXMsf1skxXUrWtesM2p1woYfQF2wihZNEqWb9jl0SPQsiqkuWG_dkdKQF64EsMCSwBcRuB2yHhk03gOHpO4AlzDfxmttH6dFiJL3aaISJfwrJONmHwxNcleJ4i2DSDT_wZ04EfIPY4oMvC6A_YZyH_i9sZfchT0PEeAx2zJhDSe_Z2tBPBh395y37e3f7YfSv291-_7272xaAqo4reVlVtpZJS1caovpFNabQeW9doaHXtBu1qV419D9q2pTFSjxIGp-yQLy-d2rLPZ9189e8VKHUz0gDTZD2ElbqyaUpVamNERj_9hz6GNfq83YmSlRa6bjL15UwNMRBFGLslYn7WsZOiOznTZWe6v85k9vrMPuMEx9fB7uFhf-54AWt6kyQ</recordid><startdate>202309</startdate><enddate>202309</enddate><creator>Barco‐Antoñanzas, Maria</creator><creator>Font‐Farre, Maria</creator><creator>Eceiza, Mikel V.</creator><creator>Gil‐Monreal, Miriam</creator><creator>van der Hoorn, Renier A. L.</creator><creator>Royuela, Mercedes</creator><creator>Zabalza, Ana</creator><general>Blackwell Publishing Ltd</general><general>Wiley Subscription Services, Inc</general><scope>24P</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7SN</scope><scope>7ST</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>SOI</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-4086-9590</orcidid><orcidid>https://orcid.org/0000-0003-4554-6798</orcidid><orcidid>https://orcid.org/0000-0002-1085-2229</orcidid><orcidid>https://orcid.org/0000-0002-6622-2234</orcidid><orcidid>https://orcid.org/0000-0002-1684-270X</orcidid><orcidid>https://orcid.org/0000-0002-3692-7487</orcidid><orcidid>https://orcid.org/0000-0001-6954-6317</orcidid></search><sort><creationdate>202309</creationdate><title>Cysteine proteases are activated in sensitive Amaranthus palmeri populations upon treatment with herbicides inhibiting amino acid biosynthesis</title><author>Barco‐Antoñanzas, Maria ; Font‐Farre, Maria ; Eceiza, Mikel V. ; Gil‐Monreal, Miriam ; van der Hoorn, Renier A. L. ; Royuela, Mercedes ; Zabalza, Ana</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3653-ba667a131137553b8182544f9d84e947dc4d7d6fbbe4a925514f1ecd3ac0012d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2023</creationdate><topic>Acetolactate synthase</topic><topic>Amaranthus palmeri</topic><topic>Amino acids</topic><topic>Biosynthesis</topic><topic>Chain branching</topic><topic>Cysteine</topic><topic>Cysteine proteinase</topic><topic>Glyphosate</topic><topic>Herbicides</topic><topic>Populations</topic><topic>Protease</topic><topic>Proteolysis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Barco‐Antoñanzas, Maria</creatorcontrib><creatorcontrib>Font‐Farre, Maria</creatorcontrib><creatorcontrib>Eceiza, Mikel V.</creatorcontrib><creatorcontrib>Gil‐Monreal, Miriam</creatorcontrib><creatorcontrib>van der Hoorn, Renier A. L.</creatorcontrib><creatorcontrib>Royuela, Mercedes</creatorcontrib><creatorcontrib>Zabalza, Ana</creatorcontrib><collection>Wiley Online Library Open Access</collection><collection>CrossRef</collection><collection>Ecology Abstracts</collection><collection>Environment Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>Environment Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Physiologia plantarum</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Barco‐Antoñanzas, Maria</au><au>Font‐Farre, Maria</au><au>Eceiza, Mikel V.</au><au>Gil‐Monreal, Miriam</au><au>van der Hoorn, Renier A. L.</au><au>Royuela, Mercedes</au><au>Zabalza, Ana</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cysteine proteases are activated in sensitive Amaranthus palmeri populations upon treatment with herbicides inhibiting amino acid biosynthesis</atitle><jtitle>Physiologia plantarum</jtitle><date>2023-09</date><risdate>2023</risdate><volume>175</volume><issue>5</issue><spage>e13993</spage><epage>n/a</epage><pages>e13993-n/a</pages><issn>0031-9317</issn><eissn>1399-3054</eissn><abstract>The herbicides glyphosate and pyrithiobac inhibit the enzyme 5‐enolpyruvylshikimate‐3‐phosphate synthase (EPSPS) in the aromatic amino acid biosynthetic pathway and acetolactate synthase (ALS) in the branched‐chain amino acid biosynthetic pathway, respectively. Here we characterise the protease activity profiles of a sensitive (S), a glyphosate‐resistant (GR) and a multiple‐resistant (MR) population of Amaranthus palmeri in response to glyphosate and pyrithiobac. Amino acid accumulation and cysteine protease activities were induced with both herbicides in the S population and with pyrithiobac in the GR population, suggesting that the increase in cysteine proteases is responsible for the increased degradation of the available proteins and the observed increase in free amino acids. Herbicides did not induce any changes in the proteolytic activities in the populations with target‐site resistance, indicating that this effect was only induced in sensitive plants.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><doi>10.1111/ppl.13993</doi><tpages>10</tpages><orcidid>https://orcid.org/0000-0002-4086-9590</orcidid><orcidid>https://orcid.org/0000-0003-4554-6798</orcidid><orcidid>https://orcid.org/0000-0002-1085-2229</orcidid><orcidid>https://orcid.org/0000-0002-6622-2234</orcidid><orcidid>https://orcid.org/0000-0002-1684-270X</orcidid><orcidid>https://orcid.org/0000-0002-3692-7487</orcidid><orcidid>https://orcid.org/0000-0001-6954-6317</orcidid><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0031-9317 |
| ispartof | Physiologia plantarum, 2023-09, Vol.175 (5), p.e13993-n/a |
| issn | 0031-9317 1399-3054 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_2882324550 |
| source | Wiley Online Library All Journals |
| subjects | Acetolactate synthase Amaranthus palmeri Amino acids Biosynthesis Chain branching Cysteine Cysteine proteinase Glyphosate Herbicides Populations Protease Proteolysis |
| title | Cysteine proteases are activated in sensitive Amaranthus palmeri populations upon treatment with herbicides inhibiting amino acid biosynthesis |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-07T06%3A25%3A33IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Cysteine%20proteases%20are%20activated%20in%20sensitive%20Amaranthus%20palmeri%20populations%20upon%20treatment%20with%20herbicides%20inhibiting%20amino%20acid%20biosynthesis&rft.jtitle=Physiologia%20plantarum&rft.au=Barco%E2%80%90Anto%C3%B1anzas,%20Maria&rft.date=2023-09&rft.volume=175&rft.issue=5&rft.spage=e13993&rft.epage=n/a&rft.pages=e13993-n/a&rft.issn=0031-9317&rft.eissn=1399-3054&rft_id=info:doi/10.1111/ppl.13993&rft_dat=%3Cproquest_cross%3E2882324550%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2881640478&rft_id=info:pmid/&rfr_iscdi=true |