14-3-3 Mediates Transcriptional Regulation by Modulating Nucleocytoplasmic Shuttling of Tobacco DNA-binding Protein Phosphatase-1
Tobacco DBP1 is the founding member of a novel class of plant transcription factors featuring sequence-specific DNA binding and protein phosphatase activity. To understand the mechanisms underlying the function of this family of transcriptional regulators, we have identified the tobacco 14-3-3 isofo...
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Veröffentlicht in: | The Journal of biological chemistry 2006-08, Vol.281 (32), p.22875-22881 |
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description | Tobacco DBP1 is the founding member of a novel class of plant transcription factors featuring sequence-specific DNA binding and protein phosphatase activity. To understand the mechanisms underlying the function of this family of transcriptional regulators, we have identified the tobacco 14-3-3 isoform G as the first protein interacting with a DBP factor. 14-3-3 recognition involves the N-terminal region of DBP1, which also supports the DNA binding activity attributed to DBP1. The relevance of this interaction is reinforced by its conservation in Arabidopsis plants, where the closest relative of DBP1 in this species also interacts with a homologous 14-3-3 protein through its N-terminal region. Furthermore, we show that in planta 14-3-3 G is directly involved in regulating DBP1 function by promoting nuclear export and subsequent cytoplasmic retention of DBP1 under conditions that in turn alleviate DBP1-mediated repression of target gene expression. |
doi_str_mv | 10.1074/jbc.M512611200 |
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To understand the mechanisms underlying the function of this family of transcriptional regulators, we have identified the tobacco 14-3-3 isoform G as the first protein interacting with a DBP factor. 14-3-3 recognition involves the N-terminal region of DBP1, which also supports the DNA binding activity attributed to DBP1. The relevance of this interaction is reinforced by its conservation in Arabidopsis plants, where the closest relative of DBP1 in this species also interacts with a homologous 14-3-3 protein through its N-terminal region. Furthermore, we show that in planta 14-3-3 G is directly involved in regulating DBP1 function by promoting nuclear export and subsequent cytoplasmic retention of DBP1 under conditions that in turn alleviate DBP1-mediated repression of target gene expression.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M512611200</identifier><identifier>PMID: 16762921</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>14-3-3 Proteins - physiology ; Agrobacterium tumefaciens - metabolism ; Arabidopsis ; DNA, Complementary - metabolism ; DNA, Plant ; DNA-Binding Proteins - biosynthesis ; DNA-Binding Proteins - physiology ; Gene Expression Regulation, Plant ; Gene Library ; Models, Biological ; Mutation ; Nicotiana - genetics ; Phosphoprotein Phosphatases - biosynthesis ; Phosphoprotein Phosphatases - physiology ; Protein Binding ; Protein Phosphatase 1 ; Protein Structure, Tertiary ; Transcription, Genetic ; Two-Hybrid System Techniques</subject><ispartof>The Journal of biological chemistry, 2006-08, Vol.281 (32), p.22875-22881</ispartof><rights>2006 © 2006 ASBMB. 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To understand the mechanisms underlying the function of this family of transcriptional regulators, we have identified the tobacco 14-3-3 isoform G as the first protein interacting with a DBP factor. 14-3-3 recognition involves the N-terminal region of DBP1, which also supports the DNA binding activity attributed to DBP1. The relevance of this interaction is reinforced by its conservation in Arabidopsis plants, where the closest relative of DBP1 in this species also interacts with a homologous 14-3-3 protein through its N-terminal region. Furthermore, we show that in planta 14-3-3 G is directly involved in regulating DBP1 function by promoting nuclear export and subsequent cytoplasmic retention of DBP1 under conditions that in turn alleviate DBP1-mediated repression of target gene expression.</description><subject>14-3-3 Proteins - physiology</subject><subject>Agrobacterium tumefaciens - metabolism</subject><subject>Arabidopsis</subject><subject>DNA, Complementary - metabolism</subject><subject>DNA, Plant</subject><subject>DNA-Binding Proteins - biosynthesis</subject><subject>DNA-Binding Proteins - physiology</subject><subject>Gene Expression Regulation, Plant</subject><subject>Gene Library</subject><subject>Models, Biological</subject><subject>Mutation</subject><subject>Nicotiana - genetics</subject><subject>Phosphoprotein Phosphatases - biosynthesis</subject><subject>Phosphoprotein Phosphatases - physiology</subject><subject>Protein Binding</subject><subject>Protein Phosphatase 1</subject><subject>Protein Structure, Tertiary</subject><subject>Transcription, Genetic</subject><subject>Two-Hybrid System Techniques</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU1v1DAQQC0EokvhyhHlgLhl8TjO17EqFJC6pYJF4mY548nGVRKntkO1R_45WXalnhC-WDN-nhnNY-w18DXwUr6_a3C9yUEUAILzJ2wFvMrSLIefT9mKcwFpLfLqjL0I4Y4vR9bwnJ1BURaiFrBiv0GmC59syFgdKSRbr8eA3k7RulH3yTfazb0-BEmzTzbO_I3GXXIzY08O99FNvQ6DxeR7N8fYH95cm2xdoxFd8uHmIm3saA7pW-8i2TG57VyYOh11oBResmet7gO9Ot3n7MfVx-3l5_T666cvlxfXKUopYookM-RNzqkRGkqsqUYOBvLSyErWjZRISEtP2dagRWkwo9YYWecmB5432Tl7d6w7eXc_U4hqsAGp7_VIbg6qqEoo8kz8F4Q6K4TM5AKujyB6F4KnVk3eDtrvFXB1sKMWO-rRzvLhzany3AxkHvGTjgV4ewQ6u-serCfVWIcdDUpUoDKhhKjKfMGqI0bLvn5Z8iqgpREXh54wKuPsv0b4A2oXqxw</recordid><startdate>20060811</startdate><enddate>20060811</enddate><creator>Carrasco, José L.</creator><creator>Castelló, María José</creator><creator>Vera, Pablo</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</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>7TM</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20060811</creationdate><title>14-3-3 Mediates Transcriptional Regulation by Modulating Nucleocytoplasmic Shuttling of Tobacco DNA-binding Protein Phosphatase-1</title><author>Carrasco, José L. ; 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To understand the mechanisms underlying the function of this family of transcriptional regulators, we have identified the tobacco 14-3-3 isoform G as the first protein interacting with a DBP factor. 14-3-3 recognition involves the N-terminal region of DBP1, which also supports the DNA binding activity attributed to DBP1. The relevance of this interaction is reinforced by its conservation in Arabidopsis plants, where the closest relative of DBP1 in this species also interacts with a homologous 14-3-3 protein through its N-terminal region. Furthermore, we show that in planta 14-3-3 G is directly involved in regulating DBP1 function by promoting nuclear export and subsequent cytoplasmic retention of DBP1 under conditions that in turn alleviate DBP1-mediated repression of target gene expression.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>16762921</pmid><doi>10.1074/jbc.M512611200</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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subjects | 14-3-3 Proteins - physiology Agrobacterium tumefaciens - metabolism Arabidopsis DNA, Complementary - metabolism DNA, Plant DNA-Binding Proteins - biosynthesis DNA-Binding Proteins - physiology Gene Expression Regulation, Plant Gene Library Models, Biological Mutation Nicotiana - genetics Phosphoprotein Phosphatases - biosynthesis Phosphoprotein Phosphatases - physiology Protein Binding Protein Phosphatase 1 Protein Structure, Tertiary Transcription, Genetic Two-Hybrid System Techniques |
title | 14-3-3 Mediates Transcriptional Regulation by Modulating Nucleocytoplasmic Shuttling of Tobacco DNA-binding Protein Phosphatase-1 |
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