Source:http://linkedlifedata.com/resource/pubmed/id/11971906
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
29
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pubmed:dateCreated |
2002-7-15
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pubmed:abstractText |
MADS-box proteins are transcription factors present in different eukaryotic kingdoms. In contrast to plants, for mammalian and yeast MADS-box proteins ternary complex formation with unrelated transcription factors was reported. We show here the first identification of such ternary interaction in plants. A rice seed-specific NF-YB was identified as partner of OsMADS18 by two-hybrid screening. NF-YB contains a histone fold motif, HFM,(1) and is part of the trimeric CCAAT-binding NF-Y complex. OsMADS18, alone or in combination with a natural partner, interacts with OsNF-YB1 through the MADS and I regions. The mouse NF-YB also associates with OsMADS18 in vivo and in vitro as a NF-YB-NF-YC dimer. Other rice MADS-box proteins do not interact in these assays, indicating specificity for the interaction. OsNF-YB1 is capable of heterodimerizing with NF-YC, but not trimerizing with NF-YA, thus precluding CCAAT binding. Mutation of the variant Asp at position 99 of the HFM alpha2-helix into a conserved serine recovers the capacity to interact with NF-YA, but not with DNA. This is the first indication that members of the NF-YB family work through mechanisms independent of the CCAAT box.
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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/CCAAT-Binding Factor,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/MADS Domain Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nfya protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Plant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
19
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pubmed:volume |
277
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
26429-35
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11971906-Amino Acid Sequence,
pubmed-meshheading:11971906-Animals,
pubmed-meshheading:11971906-Arabidopsis,
pubmed-meshheading:11971906-CCAAT-Binding Factor,
pubmed-meshheading:11971906-DNA-Binding Proteins,
pubmed-meshheading:11971906-MADS Domain Proteins,
pubmed-meshheading:11971906-Mice,
pubmed-meshheading:11971906-Molecular Sequence Data,
pubmed-meshheading:11971906-Plant Proteins,
pubmed-meshheading:11971906-Protein Binding,
pubmed-meshheading:11971906-Protein Conformation,
pubmed-meshheading:11971906-Protein Structure, Secondary,
pubmed-meshheading:11971906-Rabbits,
pubmed-meshheading:11971906-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:11971906-Sequence Alignment,
pubmed-meshheading:11971906-Transcription Factors,
pubmed-meshheading:11971906-Two-Hybrid System Techniques
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pubmed:year |
2002
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pubmed:articleTitle |
Ternary complex formation between MADS-box transcription factors and the histone fold protein NF-YB.
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pubmed:affiliation |
Dipartimento di Genetica e Biologia dei Microrganismi, Universitá di Milano, Via Celoria 26, 20133 Milano, Italy.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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