PlantRegMap/PlantTFDB v5.0
Plant Transcription Factor Database
Rosa chinensis
Species TF ID Description
RcHm_v2.0_Chr1g0318281MIKC_MADS family protein
RcHm_v2.0_Chr1g0326161MIKC_MADS family protein
RcHm_v2.0_Chr1g0351671MIKC_MADS family protein
RcHm_v2.0_Chr1g0351691MIKC_MADS family protein
RcHm_v2.0_Chr1g0376191MIKC_MADS family protein
RcHm_v2.0_Chr1g0376251MIKC_MADS family protein
RcHm_v2.0_Chr1g0376271MIKC_MADS family protein
RcHm_v2.0_Chr1g0376291MIKC_MADS family protein
RcHm_v2.0_Chr2g0100071MIKC_MADS family protein
RcHm_v2.0_Chr2g0109981MIKC_MADS family protein
RcHm_v2.0_Chr2g0110101MIKC_MADS family protein
RcHm_v2.0_Chr2g0111271MIKC_MADS family protein
RcHm_v2.0_Chr2g0151031MIKC_MADS family protein
RcHm_v2.0_Chr2g0164941MIKC_MADS family protein
RcHm_v2.0_Chr2g0164951MIKC_MADS family protein
RcHm_v2.0_Chr3g0474101MIKC_MADS family protein
RcHm_v2.0_Chr4g0429931MIKC_MADS family protein
RcHm_v2.0_Chr4g0437841MIKC_MADS family protein
RcHm_v2.0_Chr4g0437851MIKC_MADS family protein
RcHm_v2.0_Chr5g0012431MIKC_MADS family protein
RcHm_v2.0_Chr5g0020391MIKC_MADS family protein
RcHm_v2.0_Chr5g0045241MIKC_MADS family protein
RcHm_v2.0_Chr6g0296721MIKC_MADS family protein
RcHm_v2.0_Chr6g0296731MIKC_MADS family protein
RcHm_v2.0_Chr6g0302061MIKC_MADS family protein
RcHm_v2.0_Chr7g0183521MIKC_MADS family protein
RcHm_v2.0_Chr7g0183571MIKC_MADS family protein
RcHm_v2.0_Chr7g0189871MIKC_MADS family protein
RcHm_v2.0_Chr7g0199781MIKC_MADS family protein
RcHm_v2.0_Chr7g0205071MIKC_MADS family protein
RcHm_v2.0_Chr7g0229221MIKC_MADS family protein
RcHm_v2.0_Chr7g0230721MIKC_MADS family protein
RcHm_v2.0_Chr7g0236801MIKC_MADS family protein
RcHm_v2.0_Chr7g0236811MIKC_MADS family protein
RcHm_v2.0_Chr7g0240061MIKC_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