Plant Transcription Factor Database
Previous version: v3.0
Oryza barthii
M-type_MADS Family
Species TF ID Description
OBART01G07200.1M-type_MADS family protein
OBART01G12040.1M-type_MADS family protein
OBART01G12050.1M-type_MADS family protein
OBART01G14230.1M-type_MADS family protein
OBART01G14240.1M-type_MADS family protein
OBART01G14250.1M-type_MADS family protein
OBART01G14260.1M-type_MADS family protein
OBART01G40880.1M-type_MADS family protein
OBART01G41060.1M-type_MADS family protein
OBART01G41560.1M-type_MADS family protein
OBART01G42170.1M-type_MADS family protein
OBART01G45740.1M-type_MADS family protein
OBART02G04930.1M-type_MADS family protein
OBART02G21870.3M-type_MADS family protein
OBART03G01800.1M-type_MADS family protein
OBART03G10890.2M-type_MADS family protein
OBART03G23720.1M-type_MADS family protein
OBART03G23730.1M-type_MADS family protein
OBART03G24330.1M-type_MADS family protein
OBART03G39990.1M-type_MADS family protein
OBART04G08780.1M-type_MADS family protein
OBART04G10400.1M-type_MADS family protein
OBART04G10420.1M-type_MADS family protein
OBART04G15020.1M-type_MADS family protein
OBART05G10760.1M-type_MADS family protein
OBART06G00520.1M-type_MADS family protein
OBART06G00520.2M-type_MADS family protein
OBART06G00520.3M-type_MADS family protein
OBART06G07860.1M-type_MADS family protein
OBART06G07860.2M-type_MADS family protein
OBART06G13310.1M-type_MADS family protein
OBART06G14060.1M-type_MADS family protein
OBART06G16360.1M-type_MADS family protein
OBART07G02190.1M-type_MADS family protein
OBART08G15340.1M-type_MADS family protein
OBART08G15610.5M-type_MADS family protein
OBART08G19110.1M-type_MADS family protein
OBART08G19110.2M-type_MADS family protein
OBART09G00790.1M-type_MADS family protein
OBART09G00850.1M-type_MADS family protein
OBART11G21780.1M-type_MADS family protein
OBART11G21780.2M-type_MADS family protein
OBART12G09450.1M-type_MADS family protein
OBART12G09480.1M-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