pubmed-article:21323638 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:21323638 | lifeskim:mentions | umls-concept:C0162740 | lld:lifeskim |
pubmed-article:21323638 | lifeskim:mentions | umls-concept:C0205103 | lld:lifeskim |
pubmed-article:21323638 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:21323638 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
pubmed-article:21323638 | lifeskim:mentions | umls-concept:C1428954 | lld:lifeskim |
pubmed-article:21323638 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:21323638 | pubmed:dateCreated | 2011-4-13 | lld:pubmed |
pubmed-article:21323638 | pubmed:abstractText | The phytohormone gibberellin and the DELLA proteins act together to control key aspects of plant development. Gibberellin induces degradation of DELLA proteins by recruitment of an F-box protein using a molecular switch: a gibberellin-bound nuclear receptor interacts with the N-terminal domain of DELLA proteins, and this event primes the DELLA C-terminal domain for interaction with the F-box protein. However, the mechanism of signalling between the N- and C-terminal domains of DELLA proteins is unresolved. In the present study, we used in vivo and in vitro approaches to characterize di- and tri-partite interactions of the DELLA protein RGL1 (REPRESSOR OF GA1-3-LIKE 1) of Arabidopsis thaliana with the gibberellin receptor GID1A (GIBBERELLIC ACID-INSENSITIVE DWARF-1A) and the F-box protein SLY1 (SLEEPY1). Deuterium-exchange MS unequivocally showed that the entire N-terminal domain of RGL1 is disordered prior to interaction with the GID1A; furthermore, association/dissociation kinetics, determined by surface plasmon resonance, predicts a two-state conformational change of the RGL1 N-terminal domain upon interaction with GID1A. Additionally, competition assays with monoclonal antibodies revealed that contacts mediated by the short helix Asp-Glu-Leu-Leu of the hallmark DELLA motif are not essential for the GID1A-RGL1 N-terminal domain interaction. Finally, yeast two- and three-hybrid experiments determined that unabated communication between N- and C-terminal domains of RGL1 is required for recruitment of the F-box protein SLY1. | lld:pubmed |
pubmed-article:21323638 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21323638 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21323638 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21323638 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21323638 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21323638 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21323638 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21323638 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21323638 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21323638 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21323638 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21323638 | pubmed:language | eng | lld:pubmed |
pubmed-article:21323638 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21323638 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:21323638 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21323638 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21323638 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:21323638 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21323638 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:21323638 | pubmed:month | May | lld:pubmed |
pubmed-article:21323638 | pubmed:issn | 1470-8728 | lld:pubmed |
pubmed-article:21323638 | pubmed:author | pubmed-author:TurkD RDR | lld:pubmed |
pubmed-article:21323638 | pubmed:author | pubmed-author:LiShengS | lld:pubmed |
pubmed-article:21323638 | pubmed:author | pubmed-author:RakonjacJasna... | lld:pubmed |
pubmed-article:21323638 | pubmed:author | pubmed-author:FosterToshiT | lld:pubmed |
pubmed-article:21323638 | pubmed:author | pubmed-author:JonesWilliam... | lld:pubmed |
pubmed-article:21323638 | pubmed:author | pubmed-author:HarveyDawnD | lld:pubmed |
pubmed-article:21323638 | pubmed:author | pubmed-author:SunXiaolinX | lld:pubmed |
pubmed-article:21323638 | pubmed:author | pubmed-author:KirkChrisC | lld:pubmed |
pubmed-article:21323638 | pubmed:author | pubmed-author:SheerinDavid... | lld:pubmed |
pubmed-article:21323638 | pubmed:author | pubmed-author:SpagnuoloJuli... | lld:pubmed |
pubmed-article:21323638 | pubmed:author | pubmed-author:BuchananJerem... | lld:pubmed |
pubmed-article:21323638 | pubmed:author | pubmed-author:WoodsVirgil... | lld:pubmed |
pubmed-article:21323638 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:21323638 | pubmed:day | 1 | lld:pubmed |
pubmed-article:21323638 | pubmed:volume | 435 | lld:pubmed |
pubmed-article:21323638 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:21323638 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:21323638 | pubmed:pagination | 629-39 | lld:pubmed |
pubmed-article:21323638 | pubmed:dateRevised | 2011-11-1 | lld:pubmed |
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pubmed-article:21323638 | pubmed:meshHeading | pubmed-meshheading:21323638... | lld:pubmed |
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pubmed-article:21323638 | pubmed:meshHeading | pubmed-meshheading:21323638... | lld:pubmed |
pubmed-article:21323638 | pubmed:year | 2011 | lld:pubmed |
pubmed-article:21323638 | pubmed:articleTitle | Inter- and intra-molecular interactions of Arabidopsis thaliana DELLA protein RGL1. | lld:pubmed |
pubmed-article:21323638 | pubmed:affiliation | Institute of Molecular Biosciences, Massey University, Private Bag 11 222, Palmerston North, New Zealand. | lld:pubmed |
pubmed-article:21323638 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:21323638 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
pubmed-article:21323638 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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