Arabidopsis OSMOTIN 34 Functions in the ABA Signaling Pathway and Is Regulated by Proteolysis
Plants have evolutionarily established resistance responses to a variety of abiotic stress conditions, in which ABA mediates the integrated regulation of these stress responses. Numerous proteins function at the transcription level or at the protein level when contributing to controls of the ABA sig...
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Veröffentlicht in: | International journal of molecular sciences 2021-08, Vol.22 (15), p.7915 |
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description | Plants have evolutionarily established resistance responses to a variety of abiotic stress conditions, in which ABA mediates the integrated regulation of these stress responses. Numerous proteins function at the transcription level or at the protein level when contributing to controls of the ABA signaling process. Although osmotin is identified as a salt-inducible protein, its function in the abiotic stress response is yet to be elucidated. To examine the role of Arabidopsis OSMOTIN 34 (OSM34) in the ABA signaling pathway, a deletion mutant osm34 generated by a CRISPR/Cas9 system and the double mutant osm34 osml (osmotin 34-like) were analyzed for various ABA responses. Both osm34 and osm34 osml showed reduced levels of ABA responses in seeds and leaves. Moreover, proline level and expression of the proline biosynthesis gene P5CS1 was significantly reduced in osm34 osml. Interestingly, OSM34 binds to SKP2A, an F-Box protein whose transcription is induced by ABA. The protein stability of OSM34 was determined to be under the control of the 26S proteasome. In conclusion, our data suggest that OSM34 functions as a positive regulator in the generation of ABA responses and is under post-translational control. |
doi_str_mv | 10.3390/ijms22157915 |
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Numerous proteins function at the transcription level or at the protein level when contributing to controls of the ABA signaling process. Although osmotin is identified as a salt-inducible protein, its function in the abiotic stress response is yet to be elucidated. To examine the role of Arabidopsis OSMOTIN 34 (OSM34) in the ABA signaling pathway, a deletion mutant osm34 generated by a CRISPR/Cas9 system and the double mutant osm34 osml (osmotin 34-like) were analyzed for various ABA responses. Both osm34 and osm34 osml showed reduced levels of ABA responses in seeds and leaves. Moreover, proline level and expression of the proline biosynthesis gene P5CS1 was significantly reduced in osm34 osml. Interestingly, OSM34 binds to SKP2A, an F-Box protein whose transcription is induced by ABA. The protein stability of OSM34 was determined to be under the control of the 26S proteasome. In conclusion, our data suggest that OSM34 functions as a positive regulator in the generation of ABA responses and is under post-translational control.</description><identifier>ISSN: 1422-0067</identifier><identifier>ISSN: 1661-6596</identifier><identifier>EISSN: 1422-0067</identifier><identifier>DOI: 10.3390/ijms22157915</identifier><identifier>PMID: 34360680</identifier><language>eng</language><publisher>Basel: MDPI AG</publisher><subject>Abiotic stress ; Abscisic acid ; Arabidopsis ; Biosynthesis ; CRISPR ; Deletion mutant ; F-box protein ; Gene expression ; Mutants ; Mutation ; Osmotin ; Post-translation ; Proline ; Proteasome 26S ; Proteins ; Proteolysis ; Seeds ; Signal transduction ; Tobacco ; Transcription</subject><ispartof>International journal of molecular sciences, 2021-08, Vol.22 (15), p.7915</ispartof><rights>2021 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2021 by the authors. 2021</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c389t-e57cc3ebc171a7fa0be51ac5ad9526240051b256395fc9ee712040de92bdb85a3</citedby><cites>FETCH-LOGICAL-c389t-e57cc3ebc171a7fa0be51ac5ad9526240051b256395fc9ee712040de92bdb85a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC8347876/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC8347876/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids></links><search><creatorcontrib>Park, Eun-Joo</creatorcontrib><creatorcontrib>Kim, Tae-Houn</creatorcontrib><title>Arabidopsis OSMOTIN 34 Functions in the ABA Signaling Pathway and Is Regulated by Proteolysis</title><title>International journal of molecular sciences</title><description>Plants have evolutionarily established resistance responses to a variety of abiotic stress conditions, in which ABA mediates the integrated regulation of these stress responses. Numerous proteins function at the transcription level or at the protein level when contributing to controls of the ABA signaling process. Although osmotin is identified as a salt-inducible protein, its function in the abiotic stress response is yet to be elucidated. To examine the role of Arabidopsis OSMOTIN 34 (OSM34) in the ABA signaling pathway, a deletion mutant osm34 generated by a CRISPR/Cas9 system and the double mutant osm34 osml (osmotin 34-like) were analyzed for various ABA responses. Both osm34 and osm34 osml showed reduced levels of ABA responses in seeds and leaves. Moreover, proline level and expression of the proline biosynthesis gene P5CS1 was significantly reduced in osm34 osml. Interestingly, OSM34 binds to SKP2A, an F-Box protein whose transcription is induced by ABA. The protein stability of OSM34 was determined to be under the control of the 26S proteasome. In conclusion, our data suggest that OSM34 functions as a positive regulator in the generation of ABA responses and is under post-translational control.</description><subject>Abiotic stress</subject><subject>Abscisic acid</subject><subject>Arabidopsis</subject><subject>Biosynthesis</subject><subject>CRISPR</subject><subject>Deletion mutant</subject><subject>F-box protein</subject><subject>Gene expression</subject><subject>Mutants</subject><subject>Mutation</subject><subject>Osmotin</subject><subject>Post-translation</subject><subject>Proline</subject><subject>Proteasome 26S</subject><subject>Proteins</subject><subject>Proteolysis</subject><subject>Seeds</subject><subject>Signal transduction</subject><subject>Tobacco</subject><subject>Transcription</subject><issn>1422-0067</issn><issn>1661-6596</issn><issn>1422-0067</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><sourceid>8G5</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNpdkctKAzEUhoMo3nc-QMCNC6u5TCaTjVDFS0FtsbqUkMmctinTpCYzSt_e8YKoq_PD-fg4nB-hA0pOOFfk1M0XiTEqpKJiDW3TjLEeIblc_5W30E5Kc0IYZ0Jtoi2e8ZzkBdlGz_1oSleFZXIJD8d3w8fBPeYZvmq9bVzwCTuPmxng_nkfj93Um9r5KR6ZZvZmVtj4Cg8SfoBpW5sGKlyu8CiGBkK96ox7aGNi6gT733MXPV1dPl7c9G6H14OL_m3P8kI1PRDSWg6lpZIaOTGkBEGNFaZSguUsI0TQkomcKzGxCkBSRjJSgWJlVRbC8F109uVdtuUCKgu-iabWy-gWJq50ME7_3Xg309PwqgueyULmneDoWxDDSwup0QuXLNS18RDapJkQKmMdSTv08B86D23s_vJJFQUXQoqOOv6ibAwpRZj8HEOJ_uhN_-6NvwP-FIl3</recordid><startdate>20210801</startdate><enddate>20210801</enddate><creator>Park, Eun-Joo</creator><creator>Kim, Tae-Houn</creator><general>MDPI AG</general><general>MDPI</general><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>K9.</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>MBDVC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20210801</creationdate><title>Arabidopsis OSMOTIN 34 Functions in the ABA Signaling Pathway and Is Regulated by Proteolysis</title><author>Park, Eun-Joo ; Kim, Tae-Houn</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c389t-e57cc3ebc171a7fa0be51ac5ad9526240051b256395fc9ee712040de92bdb85a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>Abiotic stress</topic><topic>Abscisic acid</topic><topic>Arabidopsis</topic><topic>Biosynthesis</topic><topic>CRISPR</topic><topic>Deletion mutant</topic><topic>F-box protein</topic><topic>Gene expression</topic><topic>Mutants</topic><topic>Mutation</topic><topic>Osmotin</topic><topic>Post-translation</topic><topic>Proline</topic><topic>Proteasome 26S</topic><topic>Proteins</topic><topic>Proteolysis</topic><topic>Seeds</topic><topic>Signal transduction</topic><topic>Tobacco</topic><topic>Transcription</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Park, Eun-Joo</creatorcontrib><creatorcontrib>Kim, Tae-Houn</creatorcontrib><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>ProQuest Central</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Research Library (Corporate)</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>International journal of molecular sciences</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Park, Eun-Joo</au><au>Kim, Tae-Houn</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Arabidopsis OSMOTIN 34 Functions in the ABA Signaling Pathway and Is Regulated by Proteolysis</atitle><jtitle>International journal of molecular sciences</jtitle><date>2021-08-01</date><risdate>2021</risdate><volume>22</volume><issue>15</issue><spage>7915</spage><pages>7915-</pages><issn>1422-0067</issn><issn>1661-6596</issn><eissn>1422-0067</eissn><abstract>Plants have evolutionarily established resistance responses to a variety of abiotic stress conditions, in which ABA mediates the integrated regulation of these stress responses. Numerous proteins function at the transcription level or at the protein level when contributing to controls of the ABA signaling process. Although osmotin is identified as a salt-inducible protein, its function in the abiotic stress response is yet to be elucidated. To examine the role of Arabidopsis OSMOTIN 34 (OSM34) in the ABA signaling pathway, a deletion mutant osm34 generated by a CRISPR/Cas9 system and the double mutant osm34 osml (osmotin 34-like) were analyzed for various ABA responses. Both osm34 and osm34 osml showed reduced levels of ABA responses in seeds and leaves. Moreover, proline level and expression of the proline biosynthesis gene P5CS1 was significantly reduced in osm34 osml. Interestingly, OSM34 binds to SKP2A, an F-Box protein whose transcription is induced by ABA. The protein stability of OSM34 was determined to be under the control of the 26S proteasome. 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subjects | Abiotic stress Abscisic acid Arabidopsis Biosynthesis CRISPR Deletion mutant F-box protein Gene expression Mutants Mutation Osmotin Post-translation Proline Proteasome 26S Proteins Proteolysis Seeds Signal transduction Tobacco Transcription |
title | Arabidopsis OSMOTIN 34 Functions in the ABA Signaling Pathway and Is Regulated by Proteolysis |
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