| pubmed-article:10431823 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10431823 | lifeskim:mentions | umls-concept:C0205474 | lld:lifeskim |
| pubmed-article:10431823 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:10431823 | lifeskim:mentions | umls-concept:C1305923 | lld:lifeskim |
| pubmed-article:10431823 | lifeskim:mentions | umls-concept:C0681842 | lld:lifeskim |
| pubmed-article:10431823 | lifeskim:mentions | umls-concept:C0332462 | lld:lifeskim |
| pubmed-article:10431823 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:10431823 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:10431823 | pubmed:dateCreated | 1999-8-26 | lld:pubmed |
| pubmed-article:10431823 | pubmed:abstractText | The plant hormone indoleacetic acid (IAA or auxin) transcriptionally activates a select set of early genes. The Aux/IAA class of early auxin-responsive genes encodes a large family of short-lived, nuclear proteins. Aux/IAA polypeptides homo- and heterodimerize, and interact with auxin-response transcription factors (ARFs) via C-terminal regions conserved in both protein families. This shared region contains a predicted betaalphaalpha motif similar to the prokaryotic beta-ribbon DNA binding domain, which mediates both protein dimerization and DNA recognition. Here, we show by circular dichroism spectroscopy and by chemical cross-linking experiments that recombinant peptides corresponding to the predicted betaalphaalpha region of three Aux/IAA proteins from Arabidopsis thaliana contain substantial alpha-helical secondary structure and undergo homo- and heterotypic interactions in vitro. Our results indicate a similar biochemical function of the plant betaalphaalpha domain and suggest that the betaalphaalpha fold plays an important role in mediating combinatorial interactions of Aux/IAA and ARF proteins to specifically regulate secondary gene expression in response to auxin. | lld:pubmed |
| pubmed-article:10431823 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10431823 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10431823 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10431823 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10431823 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10431823 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10431823 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10431823 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:10431823 | pubmed:issn | 0014-5793 | lld:pubmed |
| pubmed-article:10431823 | pubmed:author | pubmed-author:MorganK EKE | lld:pubmed |
| pubmed-article:10431823 | pubmed:author | pubmed-author:AbelSS | lld:pubmed |
| pubmed-article:10431823 | pubmed:author | pubmed-author:TheologisAA | lld:pubmed |
| pubmed-article:10431823 | pubmed:author | pubmed-author:ZarembinskiT... | lld:pubmed |
| pubmed-article:10431823 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10431823 | pubmed:day | 9 | lld:pubmed |
| pubmed-article:10431823 | pubmed:volume | 454 | lld:pubmed |
| pubmed-article:10431823 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10431823 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10431823 | pubmed:pagination | 283-7 | lld:pubmed |
| pubmed-article:10431823 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:10431823 | pubmed:meshHeading | pubmed-meshheading:10431823... | lld:pubmed |
| pubmed-article:10431823 | pubmed:meshHeading | pubmed-meshheading:10431823... | lld:pubmed |
| pubmed-article:10431823 | pubmed:meshHeading | pubmed-meshheading:10431823... | lld:pubmed |
| pubmed-article:10431823 | pubmed:meshHeading | pubmed-meshheading:10431823... | lld:pubmed |
| pubmed-article:10431823 | pubmed:meshHeading | pubmed-meshheading:10431823... | lld:pubmed |
| pubmed-article:10431823 | pubmed:meshHeading | pubmed-meshheading:10431823... | lld:pubmed |
| pubmed-article:10431823 | pubmed:meshHeading | pubmed-meshheading:10431823... | lld:pubmed |
| pubmed-article:10431823 | pubmed:meshHeading | pubmed-meshheading:10431823... | lld:pubmed |
| pubmed-article:10431823 | pubmed:meshHeading | pubmed-meshheading:10431823... | lld:pubmed |
| pubmed-article:10431823 | pubmed:meshHeading | pubmed-meshheading:10431823... | lld:pubmed |
| pubmed-article:10431823 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10431823 | pubmed:articleTitle | Biochemical characterization of recombinant polypeptides corresponding to the predicted betaalphaalpha fold in Aux/IAA proteins. | lld:pubmed |
| pubmed-article:10431823 | pubmed:affiliation | Department of Vegetable Crops, University of California-Davis, 95616, USA. | lld:pubmed |
| pubmed-article:10431823 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10431823 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10431823 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10431823 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10431823 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10431823 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10431823 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10431823 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10431823 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10431823 | lld:pubmed |
