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Ternary Complex Formation between MADS-box Transcription Factors and the Histone Fold Protein NF-YB

Masiero, Simona ; Imbriano, Carol ; Ravasio, Federica ; Favaro, Rebecca ; Pelucchi, Nilla ; Gorla, Mirella Sari ; Mantovani, Roberto ; Colombo, Lucia ; Kater, Martin M.

The Journal of biological chemistry, 2002-07, Vol.277 (29), p.26429-26435 [Periódico revisado por pares]

United States: Elsevier Inc

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Ternary Complex Formation between MADS-box Transcription Factors and the Histone Fold Protein NF-YB
Autor: Masiero, Simona ; Imbriano, Carol ; Ravasio, Federica ; Favaro, Rebecca ; Pelucchi, Nilla ; Gorla, Mirella Sari ; Mantovani, Roberto ; Colombo, Lucia ; Kater, Martin M.
Assuntos: Amino Acid Sequence ; Animals ; Arabidopsis ; CCAAT-Binding Factor - metabolism ; DNA-Binding Proteins - metabolism ; MADS Domain Proteins - metabolism ; Mice ; Molecular Sequence Data ; Plant Proteins - metabolism ; Protein Binding ; Protein Conformation ; Protein Structure, Secondary ; Rabbits ; Reverse Transcriptase Polymerase Chain Reaction ; Sequence Alignment ; Transcription Factors ; Two-Hybrid System Techniques
É parte de: The Journal of biological chemistry, 2002-07, Vol.277 (29), p.26429-26435
Notas: ObjectType-Article-2
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Descrição: 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 OsMADS18in 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 α2-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.
Editor: United States: Elsevier Inc
Idioma: Inglês

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Ternary Complex Formation between MADS-box Transcription Factors and the Histone Fold Protein NF-YB

Masiero, Simona ; Imbriano, Carol ; Ravasio, Federica ; Favaro, Rebecca ; Pelucchi, Nilla ; Gorla, Mirella Sari ; Mantovani, Roberto ; Colombo, Lucia ; Kater, Martin M.

United States: Elsevier Inc

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