| pubmed-article:12646039 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12646039 | lifeskim:mentions | umls-concept:C0032098 | lld:lifeskim |
| pubmed-article:12646039 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:12646039 | lifeskim:mentions | umls-concept:C0001047 | lld:lifeskim |
| pubmed-article:12646039 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:12646039 | lifeskim:mentions | umls-concept:C1521991 | lld:lifeskim |
| pubmed-article:12646039 | lifeskim:mentions | umls-concept:C1660642 | lld:lifeskim |
| pubmed-article:12646039 | lifeskim:mentions | umls-concept:C0037791 | lld:lifeskim |
| pubmed-article:12646039 | lifeskim:mentions | umls-concept:C2826269 | lld:lifeskim |
| pubmed-article:12646039 | lifeskim:mentions | umls-concept:C0027366 | lld:lifeskim |
| pubmed-article:12646039 | pubmed:issue | Pt 1 | lld:pubmed |
| pubmed-article:12646039 | pubmed:dateCreated | 2003-3-20 | lld:pubmed |
| pubmed-article:12646039 | pubmed:abstractText | Numerous, highly conserved RING-H2 domains are found in the model plant Arabidopsis thaliana (thale cress). To characterize potential RING-H2 protein interactions, the small RING-H2 protein RHA2a was used as bait in a yeast two-hybrid screen. RHA2a interacted with one of the plant-specific NAC [NAM ('no apical meristem'), ATAF1/2, CUC2 ('cup-shaped cotyledons 2')] transcription factors, here named ANAC (abscisic acid-responsive NAC). The core RING-H2 domain was sufficient for the interaction. The ability of 11 structurally diverse RING-H2 domains to interact with ANAC was then examined. Robust interaction was detected for three of the domains, suggesting multi-specificity for the interaction. The domains that interacted with ANAC contain a glutamic acid residue in a position corresponding to a proline in many RING-H2 domains. Conversion of this glutamic acid residue into proline in RHA2a decreased its ability to interact with ANAC, most likely by changing the interaction surface. This suggested that a short, divergent region in RING-H2 domains modulate interaction specificity. ANAC contains a degenerate bipartite nuclear localization signal (NLS), while RHG1a, also identified as an ANAC interaction partner, contains a basic NLS. Both signals localized beta-glucuronidase reporter fusions to the nucleus. N-terminally truncated RHA2a also directed nuclear localization, apparently dependent on basic amino acids in the RING-H2 domain. Nuclear co-localization of the RING-H2 proteins and ANAC may enable their interaction in vivo to regulate the activity of the ANAC transcription factor. | lld:pubmed |
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| pubmed-article:12646039 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12646039 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12646039 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12646039 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:12646039 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12646039 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:12646039 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:12646039 | pubmed:author | pubmed-author:PoulsenFlemmi... | lld:pubmed |
| pubmed-article:12646039 | pubmed:author | pubmed-author:SkriverKarenK | lld:pubmed |
| pubmed-article:12646039 | pubmed:author | pubmed-author:JensenMichael... | lld:pubmed |
| pubmed-article:12646039 | pubmed:author | pubmed-author:GreveKrestine... | lld:pubmed |
| pubmed-article:12646039 | pubmed:author | pubmed-author:La CourTanjaT | lld:pubmed |
| pubmed-article:12646039 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12646039 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:12646039 | pubmed:volume | 371 | lld:pubmed |
| pubmed-article:12646039 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12646039 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12646039 | pubmed:pagination | 97-108 | lld:pubmed |
| pubmed-article:12646039 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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