Research
SEPALLATA3: the 'glue' for MADS box transcription factor complex formation
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* Corresponding author: Richard GH Immink richard.immink@wur.nl
- † Equal contributors
1 Plant Research International, Bioscience, Droevendaalsesteeg 1, Wageningen, the Netherlands
2 Wageningen University, Microspectroscopy Centre, Department of Biochemistry, Dreijenlaan 3, Wageningen, the Netherlands
3 Current address: National Laboratory of Genomics for Biodiversity (Langebio), Centro de Investigación y de Estudios Avanzados del Instituto Politécnico Nacional (CINVESTAV-IPN), Campus Guanajuato, CP 36821 Irapuato, Guanajuato, Mexico
4 Current address: Center 'Bioengineering' RAS, prospect 60-letia Oktyabrya, 7, korp. 1, 117321 Moscow, Russia
Genome Biology 2009, 10:R24 doi:10.1186/gb-2009-10-2-r24
Published: 25 February 2009Additional files
Additional data file 1:
Table S1 lists all higher-order complexes for Arabidopsis MADS domain proteins reported in the literature. Table S2 provides an overview of all MADS domain protein dimers that have been generated in yeast. Table S3 presents the higher-order complexes that were identified in the initial yeast three-hybrid screening. Table S4 lists the few dimers that could be extracted from the dataset in Additional file 3 and that were not identified before in the comprehensive two-hybrid screening [16]. Table S5 gives information about the prediction of transcription activation domains in the MADS protein sequences. Table S6 lists the yeast collection containing all SEP3ΔC2 dimers. Table S7 lists all ternary complexes that were identified using this SEP3ΔC2 collection. Figure S1 shows the data of the co-expression analysis for genes encoding interacting MADS domain proteins.
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