pubmed-article:16446457 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:16446457 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
pubmed-article:16446457 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
pubmed-article:16446457 | lifeskim:mentions | umls-concept:C1336776 | lld:lifeskim |
pubmed-article:16446457 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
pubmed-article:16446457 | pubmed:issue | 6 | lld:pubmed |
pubmed-article:16446457 | pubmed:dateCreated | 2006-2-9 | lld:pubmed |
pubmed-article:16446457 | pubmed:abstractText | bZIP-type transcription factors AREBs/ABFs bind an abscisic acid (ABA)-responsive cis-acting element named ABRE and transactivate downstream gene expression in Arabidopsis. Because AREB1 overexpression could not induce downstream gene expression, activation of AREB1 requires ABA-dependent posttranscriptional modification. We confirmed that ABA activated 42-kDa kinase activity, which, in turn, phosphorylated Ser/Thr residues of R-X-X-S/T sites in the conserved regions of AREB1. Amino acid substitutions of R-X-X-S/T sites to Ala suppressed transactivation activity, and multiple substitution of these sites resulted in almost complete suppression of transactivation activity in transient assays. In contrast, substitution of the Ser/Thr residues to Asp resulted in high transactivation activity without exogenous ABA application. A phosphorylated, transcriptionally active form was achieved by substitution of Ser/Thr in all conserved R-X-X-S/T sites to Asp. Transgenic plants overexpressing the phosphorylated active form of AREB1 expressed many ABA-inducible genes, such as RD29B, without ABA treatment. These results indicate that the ABA-dependent multisite phosphorylation of AREB1 regulates its own activation in plants. | lld:pubmed |
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pubmed-article:16446457 | pubmed:language | eng | lld:pubmed |
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pubmed-article:16446457 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:16446457 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:16446457 | pubmed:month | Feb | lld:pubmed |
pubmed-article:16446457 | pubmed:issn | 0027-8424 | lld:pubmed |
pubmed-article:16446457 | pubmed:author | pubmed-author:ShinozakiKazu... | lld:pubmed |
pubmed-article:16446457 | pubmed:author | pubmed-author:Yamaguchi-Shi... | lld:pubmed |
pubmed-article:16446457 | pubmed:author | pubmed-author:UmezawaTaishi... | lld:pubmed |
pubmed-article:16446457 | pubmed:author | pubmed-author:YoshidaRiichi... | lld:pubmed |
pubmed-article:16446457 | pubmed:author | pubmed-author:FurihataTakas... | lld:pubmed |
pubmed-article:16446457 | pubmed:author | pubmed-author:MaruyamaKyono... | lld:pubmed |
pubmed-article:16446457 | pubmed:author | pubmed-author:FujitaYasunar... | lld:pubmed |
pubmed-article:16446457 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:16446457 | pubmed:day | 7 | lld:pubmed |
pubmed-article:16446457 | pubmed:volume | 103 | lld:pubmed |
pubmed-article:16446457 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:16446457 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:16446457 | pubmed:pagination | 1988-93 | lld:pubmed |
pubmed-article:16446457 | pubmed:dateRevised | 2010-9-21 | lld:pubmed |
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pubmed-article:16446457 | pubmed:year | 2006 | lld:pubmed |
pubmed-article:16446457 | pubmed:articleTitle | Abscisic acid-dependent multisite phosphorylation regulates the activity of a transcription activator AREB1. | lld:pubmed |
pubmed-article:16446457 | pubmed:affiliation | Biological Resources Division, Japan International Research Center for Agricultural Sciences, Tsukuba, Ibaraki 305-8686, Japan. | lld:pubmed |
pubmed-article:16446457 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:16446457 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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