PlantRegMap/PlantTFDB v5.0
Plant Transcription Factor Database
Chenopodium quinoa
Species TF ID Description
AUR62002036-RAMIKC_MADS family protein
AUR62003658-RAMIKC_MADS family protein
AUR62003761-RAMIKC_MADS family protein
AUR62004272-RAMIKC_MADS family protein
AUR62004274-RAMIKC_MADS family protein
AUR62005644-RAMIKC_MADS family protein
AUR62006095-RAMIKC_MADS family protein
AUR62007715-RAMIKC_MADS family protein
AUR62007716-RAMIKC_MADS family protein
AUR62007887-RAMIKC_MADS family protein
AUR62007888-RAMIKC_MADS family protein
AUR62009424-RAMIKC_MADS family protein
AUR62009484-RAMIKC_MADS family protein
AUR62009485-RAMIKC_MADS family protein
AUR62010573-RAMIKC_MADS family protein
AUR62012889-RAMIKC_MADS family protein
AUR62013427-RAMIKC_MADS family protein
AUR62013428-RAMIKC_MADS family protein
AUR62014442-RAMIKC_MADS family protein
AUR62016454-RAMIKC_MADS family protein
AUR62017316-RAMIKC_MADS family protein
AUR62017967-RAMIKC_MADS family protein
AUR62019043-RAMIKC_MADS family protein
AUR62019397-RAMIKC_MADS family protein
AUR62022366-RAMIKC_MADS family protein
AUR62023102-RAMIKC_MADS family protein
AUR62023162-RAMIKC_MADS family protein
AUR62023163-RAMIKC_MADS family protein
AUR62024469-RAMIKC_MADS family protein
AUR62024473-RAMIKC_MADS family protein
AUR62026061-RAMIKC_MADS family protein
AUR62026062-RAMIKC_MADS family protein
AUR62026247-RAMIKC_MADS family protein
AUR62026426-RAMIKC_MADS family protein
AUR62027088-RAMIKC_MADS family protein
AUR62027090-RAMIKC_MADS family protein
AUR62027113-RAMIKC_MADS family protein
AUR62027653-RAMIKC_MADS family protein
AUR62027882-RAMIKC_MADS family protein
AUR62028906-RAMIKC_MADS family protein
AUR62030928-RAMIKC_MADS family protein
AUR62030930-RAMIKC_MADS family protein
AUR62032129-RAMIKC_MADS family protein
AUR62033383-RAMIKC_MADS family protein
AUR62033385-RAMIKC_MADS family protein
AUR62034559-RAMIKC_MADS family protein
AUR62035850-RAMIKC_MADS family protein
AUR62039676-RAMIKC_MADS family protein
AUR62042929-RAMIKC_MADS family protein
AUR62043747-RAMIKC_MADS family protein
MIKC_MADS (MIKC-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