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JXB Advance Access originally published online on May 17, 2008
Journal of Experimental Botany 2008 59(8):2253-2265; doi:10.1093/jxb/ern094
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© 2008 The Author(s).
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. This paper is available online free of all access charges (see http://jxb.oxfordjournals.org/open_access.html for further details)

RESEARCH PAPER

Interaction study of MADS-domain proteins in tomato

Charles H. Leseberg1,2, Christie L. Eissler1, Xiang Wang2, Mitrick A. Johns1, Melvin R. Duvall1 and Long Mao1,2,*

1Department of Biological Sciences, Northern Illinois University, DeKalb, IL 60115, USA
2Institute of Crop Sciences and the National Key Facility for Crop Gene Resources and Genetic Improvement, Chinese Academy of Agricultural Sciences, Beijing, 100081, PR China

* To whom correspondence should be addressed. E-mail: maolong{at}caas.net.cn

MADS-domain proteins are important transcription factors involved in many biological processes of plants. Interactions between MADS-domain proteins are essential for their functions. In tomato (Solanum lycopersicum), the number of MIKCc-type MADS-domain proteins identified has totalled 36, but a large-scale interaction assay is lacking. In this study, 22 tomato MADS-domain proteins were selected from six functionally important subfamilies of the MADS-box gene family, to create the first large-scale tomato protein interaction network. Compared with Arabidopsis and petunia (Petunia hybrida), protein interaction patterns in tomato displayed both conservation and divergence. The majority of proteins that can be identified as putative orthologues exhibited conserved interaction patterns, and modifications were mostly found in genes underlining traits unique to tomato. JOINTLESS and RIN, characterized for their roles in abscission zone development and fruit ripening, respectively, showed enlarged interaction networks in comparison with their Arabidopsis and petunia counterparts. Novel interactions were also found for members of the expanded subfamilies, such as those represented by AP1/FUL and AP3/PI MADS-domain proteins. In search for higher order complexes, TM5 was found to be the preferred bridge among the five SEP-like proteins. Additionally, 16 proteins with the MADS-domain removed were used to assess the role of the MADS-domain in protein–protein interactions. The current work provides important knowledge for further functional and evolutionary study of the MADS-box genes in tomato.

Key words: Flower development, higher order complexes, MADS-domain proteins, protein–protein interaction, tomato, yeast two-hybrid

Received 10 January 2007; Revised 6 March 2008 Accepted 6 March 2008


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