Plant Transcription Factor Database
Previous version: v3.0
Oryza nivara
M-type_MADS Family
Species TF ID Description
ONIVA01G09240.1M-type_MADS family protein
ONIVA01G14270.1M-type_MADS family protein
ONIVA01G14280.1M-type_MADS family protein
ONIVA01G16980.1M-type_MADS family protein
ONIVA01G16990.1M-type_MADS family protein
ONIVA01G46080.1M-type_MADS family protein
ONIVA01G46660.1M-type_MADS family protein
ONIVA01G48250.1M-type_MADS family protein
ONIVA01G48250.2M-type_MADS family protein
ONIVA01G48250.3M-type_MADS family protein
ONIVA01G52000.1M-type_MADS family protein
ONIVA02G05120.1M-type_MADS family protein
ONIVA02G20150.1M-type_MADS family protein
ONIVA02G24100.4M-type_MADS family protein
ONIVA03G11500.1M-type_MADS family protein
ONIVA03G12000.1M-type_MADS family protein
ONIVA03G25450.1M-type_MADS family protein
ONIVA03G25700.1M-type_MADS family protein
ONIVA03G35980.1M-type_MADS family protein
ONIVA04G01430.1M-type_MADS family protein
ONIVA04G08280.1M-type_MADS family protein
ONIVA04G08300.1M-type_MADS family protein
ONIVA04G13150.5M-type_MADS family protein
ONIVA05G11160.1M-type_MADS family protein
ONIVA06G00530.1M-type_MADS family protein
ONIVA06G09080.1M-type_MADS family protein
ONIVA06G09080.2M-type_MADS family protein
ONIVA06G15740.1M-type_MADS family protein
ONIVA06G15960.1M-type_MADS family protein
ONIVA06G16870.1M-type_MADS family protein
ONIVA06G19160.1M-type_MADS family protein
ONIVA08G16460.1M-type_MADS family protein
ONIVA08G21050.1M-type_MADS family protein
ONIVA08G21050.2M-type_MADS family protein
ONIVA09G00820.1M-type_MADS family protein
ONIVA09G00960.1M-type_MADS family protein
ONIVA10G11830.1M-type_MADS family protein
ONIVA10G11850.1M-type_MADS family protein
ONIVA12G01580.1M-type_MADS family protein
ONIVA12G01620.1M-type_MADS family protein
ONIVA12G12810.1M-type_MADS family protein
M-type_MADS (M-type MADS) Family Introduction

The best studied plant MADS-box transcription factors are those involved in floral organ identity determination. Analysis of homeotic floral mutants resulted in the formulation of a genetic model, named the ABC model, that explains how the combined functions of three classes of genes (A, B, and C) determine the identity of the four flower organs (reviewed by Coen and Meyerowitz, 1991). Arabidopsis has two A-class genes (AP1 and AP2 [Bowman et al., 1989]), two B-class genes (PI and AP3), and a single C-class gene (AG), of which only AP2 is not a MADS-box gene. Recently, it was shown that the Arabidopsis B- and C-function genes, which control petal, stamen, and carpel development, are functionally dependent on three highly similar MADS-box genes, SEP1, SEP2, and SEP3 (Pelaz et al., 2000). Interestingly, only when mutant knockout alleles of the three SEP genes were combined in a triple sep1 sep2 sep3 mutant was loss of petal, stamen, and carpel identity observed, resulting in a flower composed of only sepals. This example shows that redundancy occurs in the MADS-box gene family, which complicates reverse genetic strategies for gene function analysis. The SHP genes provide another example of MADS-box gene redundancy. shp1 and shp2 single mutants do not exhibit any phenotypic effect, whereas in the double mutant, development of the dehiscence zone is disturbed in the fruit, resulting in a failure to release seeds (Liljegren et al., 2000)[1].

It has been proposed that there are at least 2 lineages (type I and type II) of MADS-box genes in plants, animals, and fungi. Most of the well-studied plant genes are type II genes and have three more domains than type I genes from the N to the C terminus of the protein:intervening (I) domain (~30 codons), keratin-lik e coiled-coil (K) domain (~70 codons), and Cterminal (C) domain (variable length). These genes are called the MIKC-type and are specific to plants[2].

The MADS-box is a DNA binding domain of 58 amino acids that binds DNA at consensus recognition sequences known as CArG boxes [CC(A/T)6GG] (Hayes et al., 1988; Riechmann et al., 1996b). The interaction with DNA has been studied in detail for the human and yeast MADS-box proteins thanks to the resolved crystal structures (Pellegrini et al., 1995; Santelli and Richmond, 2000). The I domain is less conserved and contributes to the specification of dimerization. The K domain is characterized by a coiled-coil structure, which facilitates the dimerization of MADS-box proteins (Davies et al., 1996; Fan et al., 1997). The C domain is the least conserved domain; in some cases, it has been shown to contain a transactivation domain or to contribute to the formation of multimeric MADS-box protein complexes (Egea-Cortines et al., 1999; Honma and Goto, 2001)[1].

1.Parenicova L, de Folter S, Kieffer M, Horner DS, Favalli C, Busscher J, Cook HE, Ingram RM, Kater MM, Davies B, Angenent GC, Colombo L.
Molecular and phylogenetic analyses of the complete MADS-box transcription factor family in Arabidopsis: new openings to the MADS world.
Plant Cell. 2003 Jul;15(7):1538-51.
PMID: 12837945
2.Nam J, dePamphilis CW, Ma H, Nei M.
Antiquity and evolution of the MADS-box gene family controlling flower development in plants.
Mol Biol Evol. 2003 Sep;20(9):1435-47. Epub 2003 May 30.
PMID: 12777513