Source:http://linkedlifedata.com/resource/pubmed/id/18974936
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions |
umls-concept:C0013140,
umls-concept:C0038435,
umls-concept:C0040648,
umls-concept:C0080347,
umls-concept:C0162740,
umls-concept:C0205263,
umls-concept:C0332281,
umls-concept:C0347988,
umls-concept:C0392752,
umls-concept:C0439849,
umls-concept:C0445223,
umls-concept:C0521447,
umls-concept:C1514562,
umls-concept:C1552599,
umls-concept:C1704787,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
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| pubmed:issue |
1-2
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| pubmed:dateCreated |
2008-11-26
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| pubmed:abstractText |
HIPP26 from Arabidopsis thaliana belongs to a novel class of plant proteins, characterized by a heavy metal associated domain and an additional isoprenylation motif. It is induced during cold, salt and drought stress. The nuclear localization of HIPP26, predicted by a NLS motif, could be confirmed in onion epidermal cells overexpressing GFP-HIPP26. Experiments with modified HIPP26 indicate that the isoprenylation plays a role in the spatial distribution in the nucleus. Using promoter-GUS constructs, a tissue specific expression pattern of HIPP26 could be shown, with high expression in the vascular tissue. By a yeast-two-hybrid approach a strong interaction of HIPP26 with the zinc finger homeodomain transcription factor ATHB29, which is known to play a role in dehydration stress response could be detected. This was confirmed by GST pull-down assays. When using a modified HIPP26 lacking the two central cysteines of the heavy metal associated domain, ATHB29 was not bound in the GST pull-down assay, indicating that this structure is necessary for the interaction. Further yeast-two-hybrid analyses testing interaction of different members of the HIPP family with related zinc finger transcription factors revealed a specific interaction of ATHB29 with several HIPP proteins. A functional relationship between HIPP26 and ATHB29 is also indicated by experiments with mutants of HIPP26 showing altered expression levels of such genes known to be regulated by ATHB29.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical | |
| pubmed:status |
MEDLINE
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| pubmed:month |
Jan
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| pubmed:issn |
0167-4412
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
69
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
213-26
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| pubmed:meshHeading |
pubmed-meshheading:18974936-Arabidopsis,
pubmed-meshheading:18974936-Arabidopsis Proteins,
pubmed-meshheading:18974936-Cell Nucleus,
pubmed-meshheading:18974936-Droughts,
pubmed-meshheading:18974936-Metals, Heavy,
pubmed-meshheading:18974936-Phylogeny,
pubmed-meshheading:18974936-Protein Binding,
pubmed-meshheading:18974936-Protein Prenylation,
pubmed-meshheading:18974936-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:18974936-Transcription Factors,
pubmed-meshheading:18974936-Two-Hybrid System Techniques,
pubmed-meshheading:18974936-Zinc Fingers
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| pubmed:year |
2009
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| pubmed:articleTitle |
Stress induced and nuclear localized HIPP26 from Arabidopsis thaliana interacts via its heavy metal associated domain with the drought stress related zinc finger transcription factor ATHB29.
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| pubmed:affiliation |
Institute of Biology, Martin-Luther-University Halle-Wittenberg, Weinbergweg 10, 06120 Halle, Germany.
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| pubmed:publicationType |
Journal Article
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