Diversity of stability, localization, interaction and control of downstream gene activity in the Maize Aux/IAA protein family
AUXIN/INDOLE-3-ACETIC ACID (Aux/IAA) proteins are central regulators of auxin signal transduction. They control many aspects of plant development, share a conserved domain structure and are localized in the nucleus. In the present study, five maize Aux/IAA proteins (ZmIAA2, ZmIAA11, ZmIAA15, ZmIAA20...
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| description | AUXIN/INDOLE-3-ACETIC ACID (Aux/IAA) proteins are central regulators of auxin signal transduction. They control many aspects of plant development, share a conserved domain structure and are localized in the nucleus. In the present study, five maize Aux/IAA proteins (ZmIAA2, ZmIAA11, ZmIAA15, ZmIAA20 and ZmIAA33) representing the evolutionary, phylogenetic and expression diversity of this gene family were characterized. Subcellular localization studies revealed that ZmIAA2, ZmIAA11 and ZmIAA15 are confined to the nucleus while ZmIAA20 and ZmIAA33 are localized in both the nucleus and the cytoplasm. Introduction of specific point mutations in the degron sequence (VGWPPV) of domain II by substituting the first proline by serine or the second proline by leucine stabilized the Aux/IAA proteins. While protein half-life times between ∼11 min (ZmIAA2) to ∼120 min (ZmIAA15) were observed in wild-type proteins, the mutated forms of all five proteins were almost as stable as GFP control proteins. Moreover, all five maize Aux/IAA proteins repressed downstream gene expression in luciferase assays to different degrees. In addition, bimolecular fluorescence complementation (BiFC) analyses demonstrated interaction of all five Aux/IAA proteins with RUM1 (ROOTLESS WITH UNDETECTABLE MERISTEM 1, ZmIAA10) while only ZmIAA15 and ZmIAA33 interacted with the RUM1 paralog RUL1 (RUM-LIKE 1, ZmIAA29). Moreover, ZmIAA11, ZmIAA15 ZmIAA33 displayed homotypic interaction. Hence, despite their conserved domain structure, maize Aux/IAA proteins display a significant variability in their molecular characteristics which is likely associated with the wide spectrum of their developmental functions. |
| doi_str_mv | 10.1371/journal.pone.0107346 |
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They control many aspects of plant development, share a conserved domain structure and are localized in the nucleus. In the present study, five maize Aux/IAA proteins (ZmIAA2, ZmIAA11, ZmIAA15, ZmIAA20 and ZmIAA33) representing the evolutionary, phylogenetic and expression diversity of this gene family were characterized. Subcellular localization studies revealed that ZmIAA2, ZmIAA11 and ZmIAA15 are confined to the nucleus while ZmIAA20 and ZmIAA33 are localized in both the nucleus and the cytoplasm. Introduction of specific point mutations in the degron sequence (VGWPPV) of domain II by substituting the first proline by serine or the second proline by leucine stabilized the Aux/IAA proteins. While protein half-life times between ∼11 min (ZmIAA2) to ∼120 min (ZmIAA15) were observed in wild-type proteins, the mutated forms of all five proteins were almost as stable as GFP control proteins. Moreover, all five maize Aux/IAA proteins repressed downstream gene expression in luciferase assays to different degrees. In addition, bimolecular fluorescence complementation (BiFC) analyses demonstrated interaction of all five Aux/IAA proteins with RUM1 (ROOTLESS WITH UNDETECTABLE MERISTEM 1, ZmIAA10) while only ZmIAA15 and ZmIAA33 interacted with the RUM1 paralog RUL1 (RUM-LIKE 1, ZmIAA29). Moreover, ZmIAA11, ZmIAA15 ZmIAA33 displayed homotypic interaction. Hence, despite their conserved domain structure, maize Aux/IAA proteins display a significant variability in their molecular characteristics which is likely associated with the wide spectrum of their developmental functions.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0107346</identifier><identifier>PMID: 25203637</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Acetic acid ; Apoptosis ; Arabidopsis ; Arabidopsis - genetics ; Arabidopsis - metabolism ; Arabidopsis Proteins - genetics ; Arabidopsis Proteins - metabolism ; Arabidopsis thaliana ; Biology and Life Sciences ; Cell Nucleus - metabolism ; Cellular signal transduction ; Complementation ; Control stability ; Corn ; Crop science ; Cytoplasm ; Cytoplasm - metabolism ; Fluorescence ; Gene expression ; Gene Expression Regulation, Plant - genetics ; Gene mutation ; Genomes ; Genomics ; Half-Life ; Indoleacetic acid ; Indoleacetic Acids - metabolism ; Leucine ; Localization ; Molecular chains ; Mutation ; Nuclei ; Oryza ; Phylogenetics ; Phylogeny ; Proline ; Proteins ; Regulators ; Serine ; Transduction ; Zea mays - genetics ; Zea mays - metabolism</subject><ispartof>PloS one, 2014-09, Vol.9 (9), p.e107346-e107346</ispartof><rights>COPYRIGHT 2014 Public Library of Science</rights><rights>2014 Ludwig et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2014 Ludwig et al 2014 Ludwig et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c692t-f96c83fdfc42876bf0b861e18d3adf9a970f582514d90cf644111d2c2fe5a703</citedby><cites>FETCH-LOGICAL-c692t-f96c83fdfc42876bf0b861e18d3adf9a970f582514d90cf644111d2c2fe5a703</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/PMC4159291/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4159291/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,2102,2928,23866,27924,27925,53791,53793,79600,79601</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/25203637$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Quint, Marcel</contributor><creatorcontrib>Ludwig, Yvonne</creatorcontrib><creatorcontrib>Berendzen, Kenneth W</creatorcontrib><creatorcontrib>Xu, Changzheng</creatorcontrib><creatorcontrib>Piepho, Hans-Peter</creatorcontrib><creatorcontrib>Hochholdinger, Frank</creatorcontrib><title>Diversity of stability, localization, interaction and control of downstream gene activity in the Maize Aux/IAA protein family</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>AUXIN/INDOLE-3-ACETIC ACID (Aux/IAA) proteins are central regulators of auxin signal transduction. 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Hence, despite their conserved domain structure, maize Aux/IAA proteins display a significant variability in their molecular characteristics which is likely associated with the wide spectrum of their developmental functions.</description><subject>Acetic acid</subject><subject>Apoptosis</subject><subject>Arabidopsis</subject><subject>Arabidopsis - genetics</subject><subject>Arabidopsis - metabolism</subject><subject>Arabidopsis Proteins - genetics</subject><subject>Arabidopsis Proteins - metabolism</subject><subject>Arabidopsis thaliana</subject><subject>Biology and Life Sciences</subject><subject>Cell Nucleus - metabolism</subject><subject>Cellular signal transduction</subject><subject>Complementation</subject><subject>Control stability</subject><subject>Corn</subject><subject>Crop science</subject><subject>Cytoplasm</subject><subject>Cytoplasm - metabolism</subject><subject>Fluorescence</subject><subject>Gene expression</subject><subject>Gene Expression Regulation, Plant - genetics</subject><subject>Gene mutation</subject><subject>Genomes</subject><subject>Genomics</subject><subject>Half-Life</subject><subject>Indoleacetic acid</subject><subject>Indoleacetic Acids - metabolism</subject><subject>Leucine</subject><subject>Localization</subject><subject>Molecular chains</subject><subject>Mutation</subject><subject>Nuclei</subject><subject>Oryza</subject><subject>Phylogenetics</subject><subject>Phylogeny</subject><subject>Proline</subject><subject>Proteins</subject><subject>Regulators</subject><subject>Serine</subject><subject>Transduction</subject><subject>Zea mays - genetics</subject><subject>Zea mays - metabolism</subject><issn>1932-6203</issn><issn>1932-6203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>DOA</sourceid><recordid>eNqNk11r2zAUhs3YWLts_2BshsHYoEklS5atm0HovgIdha3sVsiylKgoUirJWVPYf5-8uCUevRi-sHX0vO-xjs7JspcQzCCq4OmV67zlZrZxVs4ABBXC5FF2DCkqpqQA6PHB91H2LIQrAEpUE_I0OyrKFCSoOs5-f9Rb6YOOu9ypPETeaJMWJ7lxght9y6N29iTXNkrPRb_IuW1z4Wz0zvSa1v2yIXrJ1_lSWpn31Lb30zaPK5l_4_pW5vPu5nQxn-cb76JMO4qvtdk9z54oboJ8Mbwn2eXnT5dnX6fnF18WZ_PzqSC0iFNFiaiRapXARV2RRoGmJlDCukW8VZTTCqiyLkqIWwqEIhhDCNtCFEqWvAJokr3e226MC2woXGCwJBBghOoyEYs90Tp-xTZer7nfMcc1-xtwfsm4j1oYyepKINliWqkCYFHRRlDEsYIpBhuo-mwfhmxds5atkKlU3IxMxztWr9jSbRmGJS0oTAbvBgPvrjsZIlvrIKQx3ErX7f8bV6CkdULf_IM-fLqBWvJ0AG2VS3lFb8rmGNYkQakbJtnsASo9rVzrdOFS6RQfCd6PBH1TyJu45F0IbPHj-_-zFz_H7NsDdiW5iavgTNd3XxiDeA8K70LwUt0XGQLWD8ldNVg_JGwYkiR7dXhB96K7qUB_ACDHDao</recordid><startdate>20140909</startdate><enddate>20140909</enddate><creator>Ludwig, Yvonne</creator><creator>Berendzen, Kenneth W</creator><creator>Xu, Changzheng</creator><creator>Piepho, Hans-Peter</creator><creator>Hochholdinger, Frank</creator><general>Public Library of Science</general><general>Public Library of Science (PLoS)</general><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>IOV</scope><scope>ISR</scope><scope>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QO</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TG</scope><scope>7TM</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PDBOC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope><scope>DOA</scope></search><sort><creationdate>20140909</creationdate><title>Diversity of stability, localization, interaction and control of downstream gene activity in the Maize Aux/IAA protein family</title><author>Ludwig, Yvonne ; Berendzen, Kenneth W ; Xu, Changzheng ; Piepho, Hans-Peter ; Hochholdinger, Frank</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c692t-f96c83fdfc42876bf0b861e18d3adf9a970f582514d90cf644111d2c2fe5a703</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Acetic acid</topic><topic>Apoptosis</topic><topic>Arabidopsis</topic><topic>Arabidopsis - 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They control many aspects of plant development, share a conserved domain structure and are localized in the nucleus. In the present study, five maize Aux/IAA proteins (ZmIAA2, ZmIAA11, ZmIAA15, ZmIAA20 and ZmIAA33) representing the evolutionary, phylogenetic and expression diversity of this gene family were characterized. Subcellular localization studies revealed that ZmIAA2, ZmIAA11 and ZmIAA15 are confined to the nucleus while ZmIAA20 and ZmIAA33 are localized in both the nucleus and the cytoplasm. Introduction of specific point mutations in the degron sequence (VGWPPV) of domain II by substituting the first proline by serine or the second proline by leucine stabilized the Aux/IAA proteins. While protein half-life times between ∼11 min (ZmIAA2) to ∼120 min (ZmIAA15) were observed in wild-type proteins, the mutated forms of all five proteins were almost as stable as GFP control proteins. Moreover, all five maize Aux/IAA proteins repressed downstream gene expression in luciferase assays to different degrees. In addition, bimolecular fluorescence complementation (BiFC) analyses demonstrated interaction of all five Aux/IAA proteins with RUM1 (ROOTLESS WITH UNDETECTABLE MERISTEM 1, ZmIAA10) while only ZmIAA15 and ZmIAA33 interacted with the RUM1 paralog RUL1 (RUM-LIKE 1, ZmIAA29). Moreover, ZmIAA11, ZmIAA15 ZmIAA33 displayed homotypic interaction. Hence, despite their conserved domain structure, maize Aux/IAA proteins display a significant variability in their molecular characteristics which is likely associated with the wide spectrum of their developmental functions.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>25203637</pmid><doi>10.1371/journal.pone.0107346</doi><oa>free_for_read</oa></addata></record> |
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| subjects | Acetic acid Apoptosis Arabidopsis Arabidopsis - genetics Arabidopsis - metabolism Arabidopsis Proteins - genetics Arabidopsis Proteins - metabolism Arabidopsis thaliana Biology and Life Sciences Cell Nucleus - metabolism Cellular signal transduction Complementation Control stability Corn Crop science Cytoplasm Cytoplasm - metabolism Fluorescence Gene expression Gene Expression Regulation, Plant - genetics Gene mutation Genomes Genomics Half-Life Indoleacetic acid Indoleacetic Acids - metabolism Leucine Localization Molecular chains Mutation Nuclei Oryza Phylogenetics Phylogeny Proline Proteins Regulators Serine Transduction Zea mays - genetics Zea mays - metabolism |
| title | Diversity of stability, localization, interaction and control of downstream gene activity in the Maize Aux/IAA protein family |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-25T09%3A33%3A27IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_plos_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Diversity%20of%20stability,%20localization,%20interaction%20and%20control%20of%20downstream%20gene%20activity%20in%20the%20Maize%20Aux/IAA%20protein%20family&rft.jtitle=PloS%20one&rft.au=Ludwig,%20Yvonne&rft.date=2014-09-09&rft.volume=9&rft.issue=9&rft.spage=e107346&rft.epage=e107346&rft.pages=e107346-e107346&rft.issn=1932-6203&rft.eissn=1932-6203&rft_id=info:doi/10.1371/journal.pone.0107346&rft_dat=%3Cgale_plos_%3EA418633836%3C/gale_plos_%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1561043385&rft_id=info:pmid/25203637&rft_galeid=A418633836&rft_doaj_id=oai_doaj_org_article_87c3ed497f204c79bc93a4f1ed41b1f0&rfr_iscdi=true |