Plant and Cell Physiology Advance Access published online on April 4, 2008
Plant and Cell Physiology, doi:10.1093/pcp/pcn059
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Interactions of B-class complex proteins involved in tepal development in Phalaenopsis orchid
1Department of Biological Sciences and Technology, National Tainan University, Tainan 700, Taiwan; 2Department of Life Sciences and 3Institute of Biotechnology, National Cheng Kung University, Tainan 701, Taiwan; 4Department of Biotechnology, South Taiwan University of Technology, Tainan County 710, Taiwan; 5Department of Life Sciences, National University of Kaohsiung, Kaohsiung 811, Taiwan
*Corresponding author, Prof. Hong-Hwa Chen. Tel: 886-6-2757575 ext. 65521, FAX: 886-6-235-6211, Email: hhchen{at}mail.ncku.edu.tw
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Abstract |
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In our previous studies, we identified four DEF-like genes and one GLO-like gene involved in floral organ development in Phalaenopsis equestris. Revealing the DNA-binding properties and protein-protein interactions of these floral homeotic MADS-box protein complexes (PeMADS) in orchids is crucial to elucidate the unique orchid floral morphogenesis. In this study, the interactome of B-class PeMADS proteins was assayed by yeast two-hybrid system (Y2H) and GST pull-down assays. Furthermore, the DNA binding activities of these proteins were assessed by using electrophoretic mobility shift assay (EMSA). All four DEF-like PeMADS proteins interacted individually with the GLO-like PeMADS6 under Y2H assay, yet with differential interaction strength. Generally, the PeMADS3/PeMADS4 lineage interacted stronger with PeMADS6 than the PeMADS2/PeMADS5 lineage did. In addition, independent homodimer formation for both PeMADS4 (DEF-like) and PeMADS6 (GLO-like) were detected. The protein-protein interactions between pairs of PeMADS proteins were further confirmed by using GST pull-down assay. Furthermore, both the PeMADS4 homodimer and the PeMADS6 homodimer/homomultimer per se were able to bind to the MADS-box protein binding motif CArG. The heterodimeric complexes of PeMADS2/PeMADS6, PeMADS4/PeMADS6 and PeMADS5/PeMADS6 showed the CArG-binding activity. Taken together, these results suggest that various complexes formed among different combinations of the five B-class PeMADS proteins may increase the complexity of their regulatory functions and thus specify the molecular basis of whorl morphogenesis and combinatorial interactions of floral organ identity genes in orchids.
Keywords: MADS-box protein - floral development - PeMADS - Phalaenopsis - protein-protein interaction
(Received October 5, 2007; Accepted March 26, 2008)
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