Plant Transcription Factor Database
Previous version: v3.0
Ocimum tenuiflorum
M-type_MADS Family
Species TF ID Description
Ote100001350021M-type_MADS family protein
Ote100003520011M-type_MADS family protein
Ote100012230151M-type_MADS family protein
Ote100012231181M-type_MADS family protein
Ote100017850041M-type_MADS family protein
Ote100019670261M-type_MADS family protein
Ote100024130021M-type_MADS family protein
Ote100039650031M-type_MADS family protein
Ote100043030001M-type_MADS family protein
Ote100086800001M-type_MADS family protein
Ote100093050051M-type_MADS family protein
Ote100093170031M-type_MADS family protein
Ote100102920111M-type_MADS family protein
Ote100106560011M-type_MADS family protein
Ote100122050061M-type_MADS family protein
Ote100145310011M-type_MADS family protein
Ote100147780061M-type_MADS family protein
Ote100150970151M-type_MADS family protein
Ote100164640001M-type_MADS family protein
Ote100168810061M-type_MADS family protein
Ote100187060031M-type_MADS family protein
Ote100193930061M-type_MADS family protein
Ote100202690041M-type_MADS family protein
Ote100210310061M-type_MADS family protein
Ote100214540101M-type_MADS family protein
Ote100214620031M-type_MADS family protein
Ote100231340001M-type_MADS family protein
Ote100236740011M-type_MADS family protein
Ote100238290051M-type_MADS family protein
Ote100239380001M-type_MADS family protein
Ote100240800031M-type_MADS family protein
Ote100244090001M-type_MADS family protein
Ote100245980001M-type_MADS family protein
Ote100252210001M-type_MADS family protein
Ote100254390021M-type_MADS family protein
Ote100254390022M-type_MADS family protein
Ote100264810051M-type_MADS family protein
Ote100269730091M-type_MADS family protein
Ote100273480001M-type_MADS family protein
Ote100274550081M-type_MADS family protein
Ote100274680051M-type_MADS family protein
Ote100275430021M-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