The SINA E3 Ligase OsDIS1 Negatively Regulates Drought Response in Rice
Ubiquitin-regulated protein degradation is a critical regulatory mechanism that controls a wide range of biological processes in plants. Here, we report that OsDISl (for Oryza sativa drought-induced SINA protein 1), a C3HC4 RING finger E3 ligase, is involved in drought-stress signal transduction in...
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| Veröffentlicht in: | Plant physiology (Bethesda) 2011-09, Vol.157 (1), p.242-255 |
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| creator | Ning, Yuese Jantasuriyarat, Chachawan Zhao, Qingzhen Zhang, Huawei Chen, Songbiao Liu, Jinling Liu, Lijing Tang, Sanyuan Park, Chan Ho Wang, Xuejun Liu, Xionglun Dai, Liangying Xie, Qi Wang, Guo-Liang |
| description | Ubiquitin-regulated protein degradation is a critical regulatory mechanism that controls a wide range of biological processes in plants. Here, we report that OsDISl (for Oryza sativa drought-induced SINA protein 1), a C3HC4 RING finger E3 ligase, is involved in drought-stress signal transduction in rice (O.sativa).The expression of OsDISl was up-regulated by drought treatment. In vitro ubiquitination assays showed that OsDISl possessed E3 ubiquitin ligase activity and that the conserved region of the RING finger was required for the activity. Transient expression assays in Nicotiana benthamiana leaves and rice protoplasts indicated that OsDISl was localized predominantly in the nucleus. Overexpression of OsDISl reduced drought tolerance in transgenic rice plants, while RNA interference silencing of OsDISl enhanced drought tolerance. Microarray analysis revealed that a large number of drought-responsive genes were induced or suppressed in the OsDISl overexpression plants under normal and drought conditions. Yeast two-hybrid screening showed that OsDISl interacted with OsNek6 (for O. sativa NIMA-related kinase 6), a tubulin complex-related serine/threonine protein kinase. Coexpression assays in N. benthamiana leaves indicated that OsNek6 was degraded by OsDISl via the 26S proteasome-dependent pathway and that this degradation was abolished by the OsDISl (H71Y) mutation, which is essential for its E3 ligase activity. Together, these results demonstrate that OsDISl plays a negative role in drought stress tolerance through transcriptional regulation of diverse stressrelated genes and possibly through posttranslational regulation of OsNek6 in rice. |
| doi_str_mv | 10.1104/pp.111.180893 |
| format | Article |
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Here, we report that OsDISl (for Oryza sativa drought-induced SINA protein 1), a C3HC4 RING finger E3 ligase, is involved in drought-stress signal transduction in rice (O.sativa).The expression of OsDISl was up-regulated by drought treatment. In vitro ubiquitination assays showed that OsDISl possessed E3 ubiquitin ligase activity and that the conserved region of the RING finger was required for the activity. Transient expression assays in Nicotiana benthamiana leaves and rice protoplasts indicated that OsDISl was localized predominantly in the nucleus. Overexpression of OsDISl reduced drought tolerance in transgenic rice plants, while RNA interference silencing of OsDISl enhanced drought tolerance. Microarray analysis revealed that a large number of drought-responsive genes were induced or suppressed in the OsDISl overexpression plants under normal and drought conditions. Yeast two-hybrid screening showed that OsDISl interacted with OsNek6 (for O. sativa NIMA-related kinase 6), a tubulin complex-related serine/threonine protein kinase. Coexpression assays in N. benthamiana leaves indicated that OsNek6 was degraded by OsDISl via the 26S proteasome-dependent pathway and that this degradation was abolished by the OsDISl (H71Y) mutation, which is essential for its E3 ligase activity. Together, these results demonstrate that OsDISl plays a negative role in drought stress tolerance through transcriptional regulation of diverse stressrelated genes and possibly through posttranslational regulation of OsNek6 in rice.</description><identifier>ISSN: 0032-0889</identifier><identifier>ISSN: 1532-2548</identifier><identifier>EISSN: 1532-2548</identifier><identifier>DOI: 10.1104/pp.111.180893</identifier><identifier>PMID: 21719639</identifier><identifier>CODEN: PPHYA5</identifier><language>eng</language><publisher>Rockville, MD: American Society of Plant Biologists</publisher><subject>Amino Acid Sequence ; Base Sequence ; Biological and medical sciences ; chemistry ; DNA Primers ; Drought ; Drought tolerance ; Droughts ; ENVIRONMENTAL STRESS AND ADAPTATION TO STRESS ; enzymology ; Fundamental and applied biological sciences. Psychology ; Gene expression regulation ; Genes ; Genes, Plant ; genetics ; leaves ; metabolism ; microarray technology ; Molecular Sequence Data ; mutation ; Nicotiana benthamiana ; Oryza ; Oryza - enzymology ; Oryza - genetics ; Oryza - physiology ; Oryza sativa ; physiology ; Plant physiology and development ; Plants ; Plants, Genetically Modified ; Plants, Genetically Modified - enzymology ; Plants, Genetically Modified - genetics ; Plants, Genetically Modified - physiology ; Plasmids ; protein degradation ; proteins ; protoplasts ; Real-Time Polymerase Chain Reaction ; Reverse Transcriptase Polymerase Chain Reaction ; Rice ; RNA ; RNA Interference ; screening ; Sequence Homology, Amino Acid ; serine ; signal transduction ; Transgenic plants ; Ubiquitin-Protein Ligases ; Ubiquitin-Protein Ligases - chemistry ; Ubiquitin-Protein Ligases - metabolism ; Ubiquitins ; yeasts</subject><ispartof>Plant physiology (Bethesda), 2011-09, Vol.157 (1), p.242-255</ispartof><rights>2011 American Society of Plant Biologists</rights><rights>2015 INIST-CNRS</rights><rights>2011 American Society of Plant Biologists. All rights reserved. 2011</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c537t-ef37a97823500b39888a6d962ddee90a4cb145c29970b4063b7257183e829da63</citedby><cites>FETCH-LOGICAL-c537t-ef37a97823500b39888a6d962ddee90a4cb145c29970b4063b7257183e829da63</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/41435502$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/41435502$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,776,780,799,881,27901,27902,57992,58225</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=24533693$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21719639$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ning, Yuese</creatorcontrib><creatorcontrib>Jantasuriyarat, Chachawan</creatorcontrib><creatorcontrib>Zhao, Qingzhen</creatorcontrib><creatorcontrib>Zhang, Huawei</creatorcontrib><creatorcontrib>Chen, Songbiao</creatorcontrib><creatorcontrib>Liu, Jinling</creatorcontrib><creatorcontrib>Liu, Lijing</creatorcontrib><creatorcontrib>Tang, Sanyuan</creatorcontrib><creatorcontrib>Park, Chan Ho</creatorcontrib><creatorcontrib>Wang, Xuejun</creatorcontrib><creatorcontrib>Liu, Xionglun</creatorcontrib><creatorcontrib>Dai, Liangying</creatorcontrib><creatorcontrib>Xie, Qi</creatorcontrib><creatorcontrib>Wang, Guo-Liang</creatorcontrib><title>The SINA E3 Ligase OsDIS1 Negatively Regulates Drought Response in Rice</title><title>Plant physiology (Bethesda)</title><addtitle>Plant Physiol</addtitle><description>Ubiquitin-regulated protein degradation is a critical regulatory mechanism that controls a wide range of biological processes in plants. Here, we report that OsDISl (for Oryza sativa drought-induced SINA protein 1), a C3HC4 RING finger E3 ligase, is involved in drought-stress signal transduction in rice (O.sativa).The expression of OsDISl was up-regulated by drought treatment. In vitro ubiquitination assays showed that OsDISl possessed E3 ubiquitin ligase activity and that the conserved region of the RING finger was required for the activity. Transient expression assays in Nicotiana benthamiana leaves and rice protoplasts indicated that OsDISl was localized predominantly in the nucleus. Overexpression of OsDISl reduced drought tolerance in transgenic rice plants, while RNA interference silencing of OsDISl enhanced drought tolerance. Microarray analysis revealed that a large number of drought-responsive genes were induced or suppressed in the OsDISl overexpression plants under normal and drought conditions. Yeast two-hybrid screening showed that OsDISl interacted with OsNek6 (for O. sativa NIMA-related kinase 6), a tubulin complex-related serine/threonine protein kinase. Coexpression assays in N. benthamiana leaves indicated that OsNek6 was degraded by OsDISl via the 26S proteasome-dependent pathway and that this degradation was abolished by the OsDISl (H71Y) mutation, which is essential for its E3 ligase activity. Together, these results demonstrate that OsDISl plays a negative role in drought stress tolerance through transcriptional regulation of diverse stressrelated genes and possibly through posttranslational regulation of OsNek6 in rice.</description><subject>Amino Acid Sequence</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>chemistry</subject><subject>DNA Primers</subject><subject>Drought</subject><subject>Drought tolerance</subject><subject>Droughts</subject><subject>ENVIRONMENTAL STRESS AND ADAPTATION TO STRESS</subject><subject>enzymology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene expression regulation</subject><subject>Genes</subject><subject>Genes, Plant</subject><subject>genetics</subject><subject>leaves</subject><subject>metabolism</subject><subject>microarray technology</subject><subject>Molecular Sequence Data</subject><subject>mutation</subject><subject>Nicotiana benthamiana</subject><subject>Oryza</subject><subject>Oryza - enzymology</subject><subject>Oryza - genetics</subject><subject>Oryza - physiology</subject><subject>Oryza sativa</subject><subject>physiology</subject><subject>Plant physiology and development</subject><subject>Plants</subject><subject>Plants, Genetically Modified</subject><subject>Plants, Genetically Modified - enzymology</subject><subject>Plants, Genetically Modified - genetics</subject><subject>Plants, Genetically Modified - physiology</subject><subject>Plasmids</subject><subject>protein degradation</subject><subject>proteins</subject><subject>protoplasts</subject><subject>Real-Time Polymerase Chain Reaction</subject><subject>Reverse Transcriptase Polymerase Chain Reaction</subject><subject>Rice</subject><subject>RNA</subject><subject>RNA Interference</subject><subject>screening</subject><subject>Sequence Homology, Amino Acid</subject><subject>serine</subject><subject>signal transduction</subject><subject>Transgenic plants</subject><subject>Ubiquitin-Protein Ligases</subject><subject>Ubiquitin-Protein Ligases - chemistry</subject><subject>Ubiquitin-Protein Ligases - metabolism</subject><subject>Ubiquitins</subject><subject>yeasts</subject><issn>0032-0889</issn><issn>1532-2548</issn><issn>1532-2548</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp90cFu1DAQBmALgehSOHIE5YLgkuLx2LF9QaraUlZatVJbzpbjeLOusklqJ5X69hh2WeDCaSzPp19jDyFvgZ4AUP55HHOFE1BUaXxGFiCQlUxw9ZwsKM1nqpQ-Iq9SuqeUAgJ_SY4YSNAV6gW5vNv44nZ5dVpcYLEKrU2-uE7ny1sornxrp_Dou6fixrdzZyefivM4zO1myjdpHPqMQ1_cBOdfkxdr2yX_Zl-PyfevF3dn38rV9eXy7HRVOoFyKv0apdVSMRSU1qiVUrZqdMWaxntNLXc1cOGY1pLWnFZYSyYkKPSK6cZWeEy-7HLHud76xvl-irYzYwxbG5_MYIP5t9OHjWmHR4NQCSUxB3zcB8ThYfZpMtuQnO862_thTkYpKYVEzrP89F8JPP8nq_JgmZY76uKQUvTrw0BAzc81mXHMFcxuTdm___sVB_17Lxl82AObnO3W0fYupD-OC8TqV9C7nbtP0xAPfQ4chaAMfwBrq6GM</recordid><startdate>20110901</startdate><enddate>20110901</enddate><creator>Ning, Yuese</creator><creator>Jantasuriyarat, Chachawan</creator><creator>Zhao, Qingzhen</creator><creator>Zhang, Huawei</creator><creator>Chen, Songbiao</creator><creator>Liu, Jinling</creator><creator>Liu, Lijing</creator><creator>Tang, Sanyuan</creator><creator>Park, Chan Ho</creator><creator>Wang, Xuejun</creator><creator>Liu, Xionglun</creator><creator>Dai, Liangying</creator><creator>Xie, Qi</creator><creator>Wang, Guo-Liang</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>7S9</scope><scope>L.6</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20110901</creationdate><title>The SINA E3 Ligase OsDIS1 Negatively Regulates Drought Response in Rice</title><author>Ning, Yuese ; Jantasuriyarat, Chachawan ; Zhao, Qingzhen ; Zhang, Huawei ; Chen, Songbiao ; Liu, Jinling ; Liu, Lijing ; Tang, Sanyuan ; Park, Chan Ho ; Wang, Xuejun ; Liu, Xionglun ; Dai, Liangying ; Xie, Qi ; Wang, Guo-Liang</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c537t-ef37a97823500b39888a6d962ddee90a4cb145c29970b4063b7257183e829da63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Amino Acid Sequence</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>chemistry</topic><topic>DNA Primers</topic><topic>Drought</topic><topic>Drought tolerance</topic><topic>Droughts</topic><topic>ENVIRONMENTAL STRESS AND ADAPTATION TO STRESS</topic><topic>enzymology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene expression regulation</topic><topic>Genes</topic><topic>Genes, Plant</topic><topic>genetics</topic><topic>leaves</topic><topic>metabolism</topic><topic>microarray technology</topic><topic>Molecular Sequence Data</topic><topic>mutation</topic><topic>Nicotiana benthamiana</topic><topic>Oryza</topic><topic>Oryza - enzymology</topic><topic>Oryza - genetics</topic><topic>Oryza - physiology</topic><topic>Oryza sativa</topic><topic>physiology</topic><topic>Plant physiology and development</topic><topic>Plants</topic><topic>Plants, Genetically Modified</topic><topic>Plants, Genetically Modified - enzymology</topic><topic>Plants, Genetically Modified - genetics</topic><topic>Plants, Genetically Modified - physiology</topic><topic>Plasmids</topic><topic>protein degradation</topic><topic>proteins</topic><topic>protoplasts</topic><topic>Real-Time Polymerase Chain Reaction</topic><topic>Reverse Transcriptase Polymerase Chain Reaction</topic><topic>Rice</topic><topic>RNA</topic><topic>RNA Interference</topic><topic>screening</topic><topic>Sequence Homology, Amino Acid</topic><topic>serine</topic><topic>signal transduction</topic><topic>Transgenic plants</topic><topic>Ubiquitin-Protein Ligases</topic><topic>Ubiquitin-Protein Ligases - chemistry</topic><topic>Ubiquitin-Protein Ligases - metabolism</topic><topic>Ubiquitins</topic><topic>yeasts</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ning, Yuese</creatorcontrib><creatorcontrib>Jantasuriyarat, Chachawan</creatorcontrib><creatorcontrib>Zhao, Qingzhen</creatorcontrib><creatorcontrib>Zhang, Huawei</creatorcontrib><creatorcontrib>Chen, Songbiao</creatorcontrib><creatorcontrib>Liu, Jinling</creatorcontrib><creatorcontrib>Liu, Lijing</creatorcontrib><creatorcontrib>Tang, Sanyuan</creatorcontrib><creatorcontrib>Park, Chan Ho</creatorcontrib><creatorcontrib>Wang, Xuejun</creatorcontrib><creatorcontrib>Liu, Xionglun</creatorcontrib><creatorcontrib>Dai, Liangying</creatorcontrib><creatorcontrib>Xie, Qi</creatorcontrib><creatorcontrib>Wang, Guo-Liang</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>AGRICOLA</collection><collection>AGRICOLA - Academic</collection><collection>MEDLINE - Academic</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>Ning, Yuese</au><au>Jantasuriyarat, Chachawan</au><au>Zhao, Qingzhen</au><au>Zhang, Huawei</au><au>Chen, Songbiao</au><au>Liu, Jinling</au><au>Liu, Lijing</au><au>Tang, Sanyuan</au><au>Park, Chan Ho</au><au>Wang, Xuejun</au><au>Liu, Xionglun</au><au>Dai, Liangying</au><au>Xie, Qi</au><au>Wang, Guo-Liang</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The SINA E3 Ligase OsDIS1 Negatively Regulates Drought Response in Rice</atitle><jtitle>Plant physiology (Bethesda)</jtitle><addtitle>Plant Physiol</addtitle><date>2011-09-01</date><risdate>2011</risdate><volume>157</volume><issue>1</issue><spage>242</spage><epage>255</epage><pages>242-255</pages><issn>0032-0889</issn><issn>1532-2548</issn><eissn>1532-2548</eissn><coden>PPHYA5</coden><abstract>Ubiquitin-regulated protein degradation is a critical regulatory mechanism that controls a wide range of biological processes in plants. Here, we report that OsDISl (for Oryza sativa drought-induced SINA protein 1), a C3HC4 RING finger E3 ligase, is involved in drought-stress signal transduction in rice (O.sativa).The expression of OsDISl was up-regulated by drought treatment. In vitro ubiquitination assays showed that OsDISl possessed E3 ubiquitin ligase activity and that the conserved region of the RING finger was required for the activity. Transient expression assays in Nicotiana benthamiana leaves and rice protoplasts indicated that OsDISl was localized predominantly in the nucleus. Overexpression of OsDISl reduced drought tolerance in transgenic rice plants, while RNA interference silencing of OsDISl enhanced drought tolerance. Microarray analysis revealed that a large number of drought-responsive genes were induced or suppressed in the OsDISl overexpression plants under normal and drought conditions. Yeast two-hybrid screening showed that OsDISl interacted with OsNek6 (for O. sativa NIMA-related kinase 6), a tubulin complex-related serine/threonine protein kinase. Coexpression assays in N. benthamiana leaves indicated that OsNek6 was degraded by OsDISl via the 26S proteasome-dependent pathway and that this degradation was abolished by the OsDISl (H71Y) mutation, which is essential for its E3 ligase activity. Together, these results demonstrate that OsDISl plays a negative role in drought stress tolerance through transcriptional regulation of diverse stressrelated genes and possibly through posttranslational regulation of OsNek6 in rice.</abstract><cop>Rockville, MD</cop><pub>American Society of Plant Biologists</pub><pmid>21719639</pmid><doi>10.1104/pp.111.180893</doi><tpages>14</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Sequence Base Sequence Biological and medical sciences chemistry DNA Primers Drought Drought tolerance Droughts ENVIRONMENTAL STRESS AND ADAPTATION TO STRESS enzymology Fundamental and applied biological sciences. Psychology Gene expression regulation Genes Genes, Plant genetics leaves metabolism microarray technology Molecular Sequence Data mutation Nicotiana benthamiana Oryza Oryza - enzymology Oryza - genetics Oryza - physiology Oryza sativa physiology Plant physiology and development Plants Plants, Genetically Modified Plants, Genetically Modified - enzymology Plants, Genetically Modified - genetics Plants, Genetically Modified - physiology Plasmids protein degradation proteins protoplasts Real-Time Polymerase Chain Reaction Reverse Transcriptase Polymerase Chain Reaction Rice RNA RNA Interference screening Sequence Homology, Amino Acid serine signal transduction Transgenic plants Ubiquitin-Protein Ligases Ubiquitin-Protein Ligases - chemistry Ubiquitin-Protein Ligases - metabolism Ubiquitins yeasts |
| title | The SINA E3 Ligase OsDIS1 Negatively Regulates Drought Response in Rice |
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