There are no files associated with this item.
Full metadata record
DC Field | Value | Language |
---|---|---|
dc.citation.endPage | 3706 | - |
dc.citation.number | 5 | - |
dc.citation.startPage | 3697 | - |
dc.citation.title | JOURNAL OF BIOLOGICAL CHEMISTRY | - |
dc.citation.volume | 280 | - |
dc.contributor.author | Yoo, JH | - |
dc.contributor.author | Park, Chan Young | - |
dc.contributor.author | Kim, JC | - |
dc.contributor.author | Heo, WD | - |
dc.contributor.author | Cheong, MS | - |
dc.contributor.author | Park, HC | - |
dc.contributor.author | Kim, MC | - |
dc.contributor.author | Moon, BC | - |
dc.contributor.author | Choi, MS | - |
dc.contributor.author | Kang, YH | - |
dc.contributor.author | Lee, JH | - |
dc.contributor.author | Kim, HS | - |
dc.contributor.author | Lee, SM | - |
dc.contributor.author | Yoon, HW | - |
dc.contributor.author | Lim, CO | - |
dc.contributor.author | Yun, DJ | - |
dc.contributor.author | Lee, SY | - |
dc.contributor.author | Chung, WS | - |
dc.contributor.author | Cho, Moo Je | - |
dc.date.accessioned | 2023-12-22T10:38:32Z | - |
dc.date.available | 2023-12-22T10:38:32Z | - |
dc.date.created | 2014-10-13 | - |
dc.date.issued | 2005-02 | - |
dc.description.abstract | Calmodulin (CaM), a ubiquitous calcium-binding protein, regulates diverse cellular functions by modulating the activity of a variety of enzymes and proteins. Plants express numerous CaM isoforms that exhibit differential activation and/or inhibition of CaM-dependent enzymes in vitro. However, the specific biological functions of plant CaM are not well known. In this study, we isolated a cDNA encoding a CaM binding transcription factor, MYB2, that regulates the expression of salt- and dehydration-responsive genes in Arabidopsis. This was achieved using a salt-inducible CaM isoform (GmCaM4) as a probe from a salt-treated Arabidopsis expression library. Using domain mapping, we identified a Ca(2+)-dependent CaM binding domain in MYB2. The specific binding of CaM to CaM binding domain was confirmed by site-directed mutagenesis, a gel mobility shift assay, split ubiquitin assay, and a competition assay using a Ca(2+)/CaM-dependent enzyme. Interestingly, the specific CaM isoform GmCaM4 enhances the DNA binding activity of AtMYB2, whereas this was inhibited by a closely related CaM isoform (GmCaM1). Overexpression of GmCaM4 in Arabidopsis up-regulates the transcription rate of AtMYB2-regulated genes, including the proline-synthesizing enzyme P5CS1 (triangle(1)-pyrroline-5-carboxylate synthetase-1), which confers salt tolerance by facilitating proline accumulation. Therefore, we suggest that a specific CaM isoform mediates salt-induced Ca(2+) signaling through the activation of an MYB transcriptional activator, thereby resulting in salt tolerance in plants. | - |
dc.identifier.bibliographicCitation | JOURNAL OF BIOLOGICAL CHEMISTRY, v.280, no.5, pp.3697 - 3706 | - |
dc.identifier.doi | 10.1074/jbc.M408237200 | - |
dc.identifier.issn | 0021-9258 | - |
dc.identifier.scopusid | 2-s2.0-13544256637 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/7191 | - |
dc.identifier.url | http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=13544256637 | - |
dc.identifier.wosid | 000226983900069 | - |
dc.language | 영어 | - |
dc.publisher | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | - |
dc.title | Direct interaction of a divergent CaM isoform and the transcription factor, MYB2, enhances salt tolerance in Arabidopsis | - |
dc.type | Article | - |
dc.description.journalRegisteredClass | scopus | - |
dc.subject.keywordPlus | DEPENDENT ENZYMES | - |
dc.subject.keywordPlus | BINDING PROTEINS | - |
dc.subject.keywordPlus | CALCIUM | - |
dc.subject.keywordPlus | THALIANA | - |
dc.subject.keywordPlus | STRESS | - |
dc.subject.keywordPlus | RECOGNITION | - |
dc.subject.keywordPlus | PLANT CALMODULIN ISOFORMS | - |
dc.subject.keywordPlus | R2R3-MYB GENE FAMILY | - |
dc.subject.keywordPlus | DIFFERENTIAL ACTIVATION | - |
dc.subject.keywordPlus | SIGNAL-TRANSDUCTION | - |
Items in Repository are protected by copyright, with all rights reserved, unless otherwise indicated.
Tel : 052-217-1404 / Email : scholarworks@unist.ac.kr
Copyright (c) 2023 by UNIST LIBRARY. All rights reserved.
ScholarWorks@UNIST was established as an OAK Project for the National Library of Korea.