Source:http://linkedlifedata.com/resource/pubmed/id/11247607
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2001-3-14
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pubmed:abstractText |
Homeodomain-leucine zipper (HDZip) proteins constitute a large family of transcription factors apparently unique to plants. In this report we characterize the DNA-binding and dimerization preferences in vitro of class I HDZip proteins. Using gel-exclusion chromatography and in vitro protein binding assays we demonstrate that the HDZip class I protein ATHB5 forms a homodimeric complex in solution. Consistent with this finding we have demonstrated the sequence-specific interaction of ATHB5 with a 9 bp pseudopalindromic DNA sequence, CAATNATTG, composed of two half-sites overlapping at a central position, by use of a PCR-assisted binding-site selection assay and competitive EMSA experiments. A majority of other known members of HDZip class I interacted with similar DNA sequences, but differed in their preference for A/T versus G/C in the central position of the binding site. Selective heterodimerization in vitro was demonstrated between ATHB5 and different class I HDZip proteins. Heterodimer formation between class I HDZip proteins is of potential functional significance for the integration of information from different signalling pathways in the control of plant development.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/HD-Zip protein, Helianthus annuus,
http://linkedlifedata.com/resource/pubmed/chemical/Homeodomain Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Plant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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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 |
45
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
63-73
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11247607-Amino Acid Sequence,
pubmed-meshheading:11247607-Arabidopsis,
pubmed-meshheading:11247607-Bacteria,
pubmed-meshheading:11247607-Base Sequence,
pubmed-meshheading:11247607-Binding Sites,
pubmed-meshheading:11247607-DNA,
pubmed-meshheading:11247607-DNA-Binding Proteins,
pubmed-meshheading:11247607-Dimerization,
pubmed-meshheading:11247607-Homeodomain Proteins,
pubmed-meshheading:11247607-Leucine Zippers,
pubmed-meshheading:11247607-Molecular Sequence Data,
pubmed-meshheading:11247607-Plant Proteins,
pubmed-meshheading:11247607-Protein Binding,
pubmed-meshheading:11247607-Recombinant Proteins,
pubmed-meshheading:11247607-Sequence Homology, Amino Acid,
pubmed-meshheading:11247607-Transcription Factors
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pubmed:year |
2001
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pubmed:articleTitle |
DNA-binding and dimerization preferences of Arabidopsis homeodomain-leucine zipper transcription factors in vitro.
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pubmed:affiliation |
Department of Evolutionary Biology, Physiological Botany, Uppsala, Sweden.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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