| pubmed-article:21487098 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:21487098 | lifeskim:mentions | umls-concept:C0162741 | lld:lifeskim |
| pubmed-article:21487098 | lifeskim:mentions | umls-concept:C0018271 | lld:lifeskim |
| pubmed-article:21487098 | lifeskim:mentions | umls-concept:C0040648 | lld:lifeskim |
| pubmed-article:21487098 | lifeskim:mentions | umls-concept:C1710076 | lld:lifeskim |
| pubmed-article:21487098 | lifeskim:mentions | umls-concept:C2587213 | lld:lifeskim |
| pubmed-article:21487098 | lifeskim:mentions | umls-concept:C1527118 | lld:lifeskim |
| pubmed-article:21487098 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:21487098 | pubmed:dateCreated | 2011-5-27 | lld:pubmed |
| pubmed-article:21487098 | pubmed:abstractText | Plants contain ?-amylase-like proteins (BAMs; enzymes usually associated with starch breakdown) present in the nucleus rather than targeted to the chloroplast. They possess BRASSINAZOLE RESISTANT1 (BZR1)-type DNA binding domains--also found in transcription factors mediating brassinosteroid (BR) responses. The two Arabidopsis thaliana BZR1-BAM proteins (BAM7 and BAM8) bind a cis-regulatory element that both contains a G box and resembles a BR-responsive element. In protoplast transactivation assays, these BZR1-BAMs activate gene expression. Structural modeling suggests that the BAM domain's glucan binding cleft is intact, but the recombinant proteins are at least 1000 times less active than chloroplastic ?-amylases. Deregulation of BZR1-BAMs (the bam7bam8 double mutant and BAM8-overexpressing plants) causes altered leaf growth and development. Of the genes upregulated in plants overexpressing BAM8 and downregulated in bam7bam8 plants, many carry the cis-regulatory element in their promoters. Many genes that respond to BRs are inversely regulated by BZR1-BAMs. We propose a role for BZR1-BAMs in controlling plant growth and development through crosstalk with BR signaling. Furthermore, we speculate that BZR1-BAMs may transmit metabolic signals by binding a ligand in their BAM domain, although diurnal changes in the concentration of maltose, a candidate ligand produced by chloroplastic ?-amylases, do not influence their transcription factor function. | lld:pubmed |
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| pubmed-article:21487098 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:21487098 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:21487098 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:21487098 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:21487098 | pubmed:issn | 1532-298X | lld:pubmed |
| pubmed-article:21487098 | pubmed:author | pubmed-author:ZeemanSamuel... | lld:pubmed |
| pubmed-article:21487098 | pubmed:author | pubmed-author:VaughanCara... | lld:pubmed |
| pubmed-article:21487098 | pubmed:author | pubmed-author:MonroeJonatha... | lld:pubmed |
| pubmed-article:21487098 | pubmed:author | pubmed-author:ReinholdHeike... | lld:pubmed |
| pubmed-article:21487098 | pubmed:author | pubmed-author:SoykSebastian... | lld:pubmed |
| pubmed-article:21487098 | pubmed:author | pubmed-author:SimkováKláraK | lld:pubmed |
| pubmed-article:21487098 | pubmed:author | pubmed-author:HostettlerCar... | lld:pubmed |
| pubmed-article:21487098 | pubmed:author | pubmed-author:MarafinoJohnJ | lld:pubmed |
| pubmed-article:21487098 | pubmed:author | pubmed-author:MainieroSaman... | lld:pubmed |
| pubmed-article:21487098 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:21487098 | pubmed:volume | 23 | lld:pubmed |
| pubmed-article:21487098 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:21487098 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:21487098 | pubmed:pagination | 1391-403 | lld:pubmed |
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