Arabidopsis nitrate reductase activity is stimulated by the E3 SUMO ligase AtSIZ1
Small ubiquitin-related modifier (SUMO) is a small polypeptide that modulates protein activity and regulates hormone signalling, abiotic and biotic responses in plants. Here we show that AtSIZ regulates nitrogen assimilation in Arabidopsis through its E3 SUMO ligase function. Dwarf plants of siz1-2...
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| Veröffentlicht in: | Nature communications 2011-07, Vol.2 (1), p.400-400, Article 400 |
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| description | Small ubiquitin-related modifier (SUMO) is a small polypeptide that modulates protein activity and regulates hormone signalling, abiotic and biotic responses in plants. Here we show that AtSIZ regulates nitrogen assimilation in
Arabidopsis
through its E3 SUMO ligase function. Dwarf plants of
siz1-2
flower early, show abnormal seed development and have high salicylic acid content and enhanced resistance to bacterial pathogens. These mutant phenotypes are reverted to wild-type phenotypes by exogenous ammonium but not by nitrate, phosphate or potassium. Decreased nitrate reductase activity in
siz1-2
plants resulted in low nitrogen concentrations, low nitric oxide production and high nitrate content in comparison with wild-type plants. The nitrate reductases, NIA1 and NIA2, are sumoylated by AtSIZ1, which dramatically increases their activity. Both sumoylated and non-sumoylated NIA1 and NIA2 can form dimers. Our results indicate that AtSIZ1 positively controls nitrogen assimilation by promoting sumoylation of NRs in
Arabidopsis
.
Posttranslational modification of proteins by small ubiquitin-related modifier is a response to stress signalling in plants. Here, the
Arabdiposis
protein SIZ1 is shown to cause SUMOylation of nitrate reductases 1 and 2 and to increase their activity, suggesting that SIZ1 controls nitrate uptake via SUMOylation. |
| doi_str_mv | 10.1038/ncomms1408 |
| format | Article |
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Arabidopsis
through its E3 SUMO ligase function. Dwarf plants of
siz1-2
flower early, show abnormal seed development and have high salicylic acid content and enhanced resistance to bacterial pathogens. These mutant phenotypes are reverted to wild-type phenotypes by exogenous ammonium but not by nitrate, phosphate or potassium. Decreased nitrate reductase activity in
siz1-2
plants resulted in low nitrogen concentrations, low nitric oxide production and high nitrate content in comparison with wild-type plants. The nitrate reductases, NIA1 and NIA2, are sumoylated by AtSIZ1, which dramatically increases their activity. Both sumoylated and non-sumoylated NIA1 and NIA2 can form dimers. Our results indicate that AtSIZ1 positively controls nitrogen assimilation by promoting sumoylation of NRs in
Arabidopsis
.
Posttranslational modification of proteins by small ubiquitin-related modifier is a response to stress signalling in plants. Here, the
Arabdiposis
protein SIZ1 is shown to cause SUMOylation of nitrate reductases 1 and 2 and to increase their activity, suggesting that SIZ1 controls nitrate uptake via SUMOylation.</description><identifier>ISSN: 2041-1723</identifier><identifier>EISSN: 2041-1723</identifier><identifier>DOI: 10.1038/ncomms1408</identifier><identifier>PMID: 21772271</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>631/337/458/538 ; 631/449/1736 ; 631/449/2653 ; 631/45/612/645 ; Arabidopsis - enzymology ; Arabidopsis - immunology ; Arabidopsis - metabolism ; Arabidopsis - microbiology ; Arabidopsis Proteins - genetics ; Arabidopsis Proteins - metabolism ; Colony Count, Microbial ; Humanities and Social Sciences ; Ligases - genetics ; Ligases - metabolism ; multidisciplinary ; Mutation - genetics ; Nitrate Reductase - chemistry ; Nitrate Reductase - metabolism ; Nitrates - analysis ; Nitric Oxide - biosynthesis ; Protein Multimerization ; Pseudomonas syringae - immunology ; Quaternary Ammonium Compounds - pharmacology ; Salicylic Acid - analysis ; Science ; Science (multidisciplinary) ; Seeds - chemistry ; Small Ubiquitin-Related Modifier Proteins - metabolism ; Sumoylation ; Ubiquitin-Protein Ligases - metabolism</subject><ispartof>Nature communications, 2011-07, Vol.2 (1), p.400-400, Article 400</ispartof><rights>The Author(s) 2011</rights><rights>Copyright Nature Publishing Group Jul 2011</rights><rights>Copyright © 2011, Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved. 2011 Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c506t-bee007c2912b413faad6914df7ae4da9459a2b8398e649afc2fc90941ec60f6f3</citedby><cites>FETCH-LOGICAL-c506t-bee007c2912b413faad6914df7ae4da9459a2b8398e649afc2fc90941ec60f6f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/ncomms1408$$EPDF$$P50$$Gspringer$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://doi.org/10.1038/ncomms1408$$EHTML$$P50$$Gspringer$$Hfree_for_read</linktohtml><link.rule.ids>230,314,776,780,881,27903,27904,41099,42168,51554</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21772271$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Park, Bong Soo</creatorcontrib><creatorcontrib>Song, Jong Tae</creatorcontrib><creatorcontrib>Seo, Hak Soo</creatorcontrib><title>Arabidopsis nitrate reductase activity is stimulated by the E3 SUMO ligase AtSIZ1</title><title>Nature communications</title><addtitle>Nat Commun</addtitle><addtitle>Nat Commun</addtitle><description>Small ubiquitin-related modifier (SUMO) is a small polypeptide that modulates protein activity and regulates hormone signalling, abiotic and biotic responses in plants. Here we show that AtSIZ regulates nitrogen assimilation in
Arabidopsis
through its E3 SUMO ligase function. Dwarf plants of
siz1-2
flower early, show abnormal seed development and have high salicylic acid content and enhanced resistance to bacterial pathogens. These mutant phenotypes are reverted to wild-type phenotypes by exogenous ammonium but not by nitrate, phosphate or potassium. Decreased nitrate reductase activity in
siz1-2
plants resulted in low nitrogen concentrations, low nitric oxide production and high nitrate content in comparison with wild-type plants. The nitrate reductases, NIA1 and NIA2, are sumoylated by AtSIZ1, which dramatically increases their activity. Both sumoylated and non-sumoylated NIA1 and NIA2 can form dimers. Our results indicate that AtSIZ1 positively controls nitrogen assimilation by promoting sumoylation of NRs in
Arabidopsis
.
Posttranslational modification of proteins by small ubiquitin-related modifier is a response to stress signalling in plants. Here, the
Arabdiposis
protein SIZ1 is shown to cause SUMOylation of nitrate reductases 1 and 2 and to increase their activity, suggesting that SIZ1 controls nitrate uptake via SUMOylation.</description><subject>631/337/458/538</subject><subject>631/449/1736</subject><subject>631/449/2653</subject><subject>631/45/612/645</subject><subject>Arabidopsis - enzymology</subject><subject>Arabidopsis - immunology</subject><subject>Arabidopsis - metabolism</subject><subject>Arabidopsis - microbiology</subject><subject>Arabidopsis Proteins - genetics</subject><subject>Arabidopsis Proteins - metabolism</subject><subject>Colony Count, Microbial</subject><subject>Humanities and Social Sciences</subject><subject>Ligases - genetics</subject><subject>Ligases - metabolism</subject><subject>multidisciplinary</subject><subject>Mutation - genetics</subject><subject>Nitrate Reductase - chemistry</subject><subject>Nitrate Reductase - metabolism</subject><subject>Nitrates - analysis</subject><subject>Nitric Oxide - biosynthesis</subject><subject>Protein Multimerization</subject><subject>Pseudomonas syringae - immunology</subject><subject>Quaternary Ammonium Compounds - pharmacology</subject><subject>Salicylic Acid - analysis</subject><subject>Science</subject><subject>Science (multidisciplinary)</subject><subject>Seeds - chemistry</subject><subject>Small Ubiquitin-Related Modifier Proteins - metabolism</subject><subject>Sumoylation</subject><subject>Ubiquitin-Protein Ligases - metabolism</subject><issn>2041-1723</issn><issn>2041-1723</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>C6C</sourceid><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNptkV9LHDEUxYO0uGL3xQ9QQl8Klq25mewkeSksYqugiOi--BIymTtrZP5sk4yw376RVdeW5uUGzo9zz-UQcgTsO7BCnfRu6LoIgqk9csCZgBlIXnx495-QaYyPLL9CgxJin0w4SMm5hANyswi28vWwjj7S3qdgE9KA9eiSjUitS_7Jpw3Naky-G9us17Ta0PSA9Kygt8ura9r61TO8SLcX9_CJfGxsG3H6Mg_J8ufZ3en57PL618Xp4nLm5qxMswqRMem4Bl4JKBpr61KDqBtpUdRWi7m2vFKFVlgKbRvHG6eZFoCuZE3ZFIfkx9Z3PVYd1g77HL416-A7GzZmsN78rfT-wayGJ1NAyUCU2eDri0EYfo8Yk-l8dNi2tsdhjEZJNddzqVUmv_xDPg5j6PN1RmkhgWnQGTreQi4MMQZs3qIAM89VmV1VGf78Pvwb-lpMBr5tgZilfoVht_I_dn8Al9Oe_Q</recordid><startdate>20110719</startdate><enddate>20110719</enddate><creator>Park, Bong Soo</creator><creator>Song, Jong Tae</creator><creator>Seo, Hak Soo</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</general><scope>C6C</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>3V.</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7ST</scope><scope>7T5</scope><scope>7T7</scope><scope>7TM</scope><scope>7TO</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</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>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>RC3</scope><scope>SOI</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20110719</creationdate><title>Arabidopsis nitrate reductase activity is stimulated by the E3 SUMO ligase AtSIZ1</title><author>Park, Bong Soo ; Song, Jong Tae ; Seo, Hak Soo</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c506t-bee007c2912b413faad6914df7ae4da9459a2b8398e649afc2fc90941ec60f6f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>631/337/458/538</topic><topic>631/449/1736</topic><topic>631/449/2653</topic><topic>631/45/612/645</topic><topic>Arabidopsis - 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metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Park, Bong Soo</creatorcontrib><creatorcontrib>Song, Jong Tae</creatorcontrib><creatorcontrib>Seo, Hak Soo</creatorcontrib><collection>Springer Nature OA Free Journals</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Environment Abstracts</collection><collection>Immunology Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>ProQuest Health and Medical</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>Advanced Technologies & Aerospace Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection (ProQuest)</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>ProQuest Biological Science Journals</collection><collection>Advanced Technologies & Aerospace Database</collection><collection>ProQuest Advanced Technologies & Aerospace Collection</collection><collection>Biotechnology and BioEngineering Abstracts</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>Genetics Abstracts</collection><collection>Environment Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Nature communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Park, Bong Soo</au><au>Song, Jong Tae</au><au>Seo, Hak Soo</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Arabidopsis nitrate reductase activity is stimulated by the E3 SUMO ligase AtSIZ1</atitle><jtitle>Nature communications</jtitle><stitle>Nat Commun</stitle><addtitle>Nat Commun</addtitle><date>2011-07-19</date><risdate>2011</risdate><volume>2</volume><issue>1</issue><spage>400</spage><epage>400</epage><pages>400-400</pages><artnum>400</artnum><issn>2041-1723</issn><eissn>2041-1723</eissn><abstract>Small ubiquitin-related modifier (SUMO) is a small polypeptide that modulates protein activity and regulates hormone signalling, abiotic and biotic responses in plants. Here we show that AtSIZ regulates nitrogen assimilation in
Arabidopsis
through its E3 SUMO ligase function. Dwarf plants of
siz1-2
flower early, show abnormal seed development and have high salicylic acid content and enhanced resistance to bacterial pathogens. These mutant phenotypes are reverted to wild-type phenotypes by exogenous ammonium but not by nitrate, phosphate or potassium. Decreased nitrate reductase activity in
siz1-2
plants resulted in low nitrogen concentrations, low nitric oxide production and high nitrate content in comparison with wild-type plants. The nitrate reductases, NIA1 and NIA2, are sumoylated by AtSIZ1, which dramatically increases their activity. Both sumoylated and non-sumoylated NIA1 and NIA2 can form dimers. Our results indicate that AtSIZ1 positively controls nitrogen assimilation by promoting sumoylation of NRs in
Arabidopsis
.
Posttranslational modification of proteins by small ubiquitin-related modifier is a response to stress signalling in plants. Here, the
Arabdiposis
protein SIZ1 is shown to cause SUMOylation of nitrate reductases 1 and 2 and to increase their activity, suggesting that SIZ1 controls nitrate uptake via SUMOylation.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>21772271</pmid><doi>10.1038/ncomms1408</doi><tpages>1</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | 631/337/458/538 631/449/1736 631/449/2653 631/45/612/645 Arabidopsis - enzymology Arabidopsis - immunology Arabidopsis - metabolism Arabidopsis - microbiology Arabidopsis Proteins - genetics Arabidopsis Proteins - metabolism Colony Count, Microbial Humanities and Social Sciences Ligases - genetics Ligases - metabolism multidisciplinary Mutation - genetics Nitrate Reductase - chemistry Nitrate Reductase - metabolism Nitrates - analysis Nitric Oxide - biosynthesis Protein Multimerization Pseudomonas syringae - immunology Quaternary Ammonium Compounds - pharmacology Salicylic Acid - analysis Science Science (multidisciplinary) Seeds - chemistry Small Ubiquitin-Related Modifier Proteins - metabolism Sumoylation Ubiquitin-Protein Ligases - metabolism |
| title | Arabidopsis nitrate reductase activity is stimulated by the E3 SUMO ligase AtSIZ1 |
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