{"title":"拟南芥NAC域转录激活因子VND7负向调控VNI2的表达。","authors":"Aili Ailizati, Isura Sumeda Priyadarshana Nagahage, Atsuko Miyagi, Toshiki Ishikawa, Maki Kawai-Yamada, Taku Demura, Masatoshi Yamaguchi","doi":"10.5511/plantbiotechnology.21.1013a","DOIUrl":null,"url":null,"abstract":"<p><p>A NAC domain transcription factor, VND-INTERACTING2 (VNI2) is originally isolated as an interacting protein with another NAC domain transcription factor, VASCULAR-RELATED NAC-DOMAIN7 (VND7), a master regulator of xylem vessel element differentiation. VND7 directly or indirectly induces expression of a number of genes associated with xylem vessel element differentiation, while VNI2 inhibits the transcriptional activation activities of VND7 by forming a protein complex. <i>VNI2</i> is expressed at an earlier stage of xylem vessel element differentiation than <i>VND7</i>. Here, to investigate whether VND7 also affects VNI2, a transient expression assay was performed. We demonstrated that VND7 downregulated <i>VNI2</i> expression. Other transcription factors involved in xylem vessel formation did not show the negative regulation of <i>VNI2</i> expression. Rather, MYB83, a downstream target of VND7, upregulated <i>VNI2</i> expression. By using the deletion series of the <i>VNI2</i> promoter, a 400 bp region was identified as being responsible for downregulation by VND7. These data suggested that VND7 and VNI2 mutually regulate each other, and <i>VNI2</i> expression is both positively and negatively regulated in the transcriptional cascade.</p>","PeriodicalId":1,"journal":{"name":"Accounts of Chemical Research","volume":null,"pages":null},"PeriodicalIF":16.4000,"publicationDate":"2021-12-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8761584/pdf/plantbiotechnology-38-4-21.1013a.pdf","citationCount":"3","resultStr":"{\"title\":\"An Arabidopsis NAC domain transcriptional activator VND7 negatively regulates <i>VNI2</i> expression.\",\"authors\":\"Aili Ailizati, Isura Sumeda Priyadarshana Nagahage, Atsuko Miyagi, Toshiki Ishikawa, Maki Kawai-Yamada, Taku Demura, Masatoshi Yamaguchi\",\"doi\":\"10.5511/plantbiotechnology.21.1013a\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>A NAC domain transcription factor, VND-INTERACTING2 (VNI2) is originally isolated as an interacting protein with another NAC domain transcription factor, VASCULAR-RELATED NAC-DOMAIN7 (VND7), a master regulator of xylem vessel element differentiation. VND7 directly or indirectly induces expression of a number of genes associated with xylem vessel element differentiation, while VNI2 inhibits the transcriptional activation activities of VND7 by forming a protein complex. <i>VNI2</i> is expressed at an earlier stage of xylem vessel element differentiation than <i>VND7</i>. Here, to investigate whether VND7 also affects VNI2, a transient expression assay was performed. We demonstrated that VND7 downregulated <i>VNI2</i> expression. Other transcription factors involved in xylem vessel formation did not show the negative regulation of <i>VNI2</i> expression. Rather, MYB83, a downstream target of VND7, upregulated <i>VNI2</i> expression. By using the deletion series of the <i>VNI2</i> promoter, a 400 bp region was identified as being responsible for downregulation by VND7. These data suggested that VND7 and VNI2 mutually regulate each other, and <i>VNI2</i> expression is both positively and negatively regulated in the transcriptional cascade.</p>\",\"PeriodicalId\":1,\"journal\":{\"name\":\"Accounts of Chemical Research\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":16.4000,\"publicationDate\":\"2021-12-25\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8761584/pdf/plantbiotechnology-38-4-21.1013a.pdf\",\"citationCount\":\"3\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Accounts of Chemical Research\",\"FirstCategoryId\":\"5\",\"ListUrlMain\":\"https://doi.org/10.5511/plantbiotechnology.21.1013a\",\"RegionNum\":1,\"RegionCategory\":\"化学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"CHEMISTRY, MULTIDISCIPLINARY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Accounts of Chemical Research","FirstCategoryId":"5","ListUrlMain":"https://doi.org/10.5511/plantbiotechnology.21.1013a","RegionNum":1,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"CHEMISTRY, MULTIDISCIPLINARY","Score":null,"Total":0}
A NAC domain transcription factor, VND-INTERACTING2 (VNI2) is originally isolated as an interacting protein with another NAC domain transcription factor, VASCULAR-RELATED NAC-DOMAIN7 (VND7), a master regulator of xylem vessel element differentiation. VND7 directly or indirectly induces expression of a number of genes associated with xylem vessel element differentiation, while VNI2 inhibits the transcriptional activation activities of VND7 by forming a protein complex. VNI2 is expressed at an earlier stage of xylem vessel element differentiation than VND7. Here, to investigate whether VND7 also affects VNI2, a transient expression assay was performed. We demonstrated that VND7 downregulated VNI2 expression. Other transcription factors involved in xylem vessel formation did not show the negative regulation of VNI2 expression. Rather, MYB83, a downstream target of VND7, upregulated VNI2 expression. By using the deletion series of the VNI2 promoter, a 400 bp region was identified as being responsible for downregulation by VND7. These data suggested that VND7 and VNI2 mutually regulate each other, and VNI2 expression is both positively and negatively regulated in the transcriptional cascade.
期刊介绍:
Accounts of Chemical Research presents short, concise and critical articles offering easy-to-read overviews of basic research and applications in all areas of chemistry and biochemistry. These short reviews focus on research from the author’s own laboratory and are designed to teach the reader about a research project. In addition, Accounts of Chemical Research publishes commentaries that give an informed opinion on a current research problem. Special Issues online are devoted to a single topic of unusual activity and significance.
Accounts of Chemical Research replaces the traditional article abstract with an article "Conspectus." These entries synopsize the research affording the reader a closer look at the content and significance of an article. Through this provision of a more detailed description of the article contents, the Conspectus enhances the article's discoverability by search engines and the exposure for the research.