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dc.contributor.authorDuvall, Melvin R.
dc.contributor.authorLeseberg, Charles H.
dc.contributor.authorEissler, Christie
dc.contributor.authorWang, Xiang
dc.contributor.authorJohns, Mitrick A.
dc.contributor.authorMao, Long
dc.date.accessioned2013-02-12T17:06:23Z
dc.date.available2013-02-12T17:06:23Z
dc.date.issued2008-05
dc.identifier.citationLeseberg, C., C. Eissler, X. Wang, M. Johns, M. Duvall and L. Mao. 2008. Interaction study of MADS domain proteins in tomato. Journal of Experimental Botany 59: 2253-2265.en_US
dc.identifier.issn0022-0957
dc.identifier.urihttp://commons.lib.niu.edu/handle/10843/13416
dc.identifier.urihttp://hdl.handle.net/10843/13416
dc.description.abstractMADS-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 MADSdomain proteins identified has totalled 36, but a largescale 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 MADSbox genes in tomato.en_US
dc.language.isoen_USen_US
dc.publisherOxford University Pressen_US
dc.subjectFlower developmenten_US
dc.subjecthigher order complexesen_US
dc.subjectMADS-domain proteinsen_US
dc.subjectprotein-protein interactionen_US
dc.subjecttomatoen_US
dc.subjectyeast two-hybriden_US
dc.titleInteraction Study of MADS-Domain Proteins in Tomatoen_US
dc.typeArticleen_US
dc.altlocation.urihttp://dx.doi.org/10.1093/jxb/ern094en_US
dc.contributor.departmentDepartment of Biological Sciences


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