The MADS-Box Family of Transcription Factors
Article first published online: 3 MAR 2005
European Journal of Biochemistry
Volume 229, Issue 1, pages 1–13, April 1995
How to Cite
Shore, P. and Sharrocks, A. D. (1995), The MADS-Box Family of Transcription Factors. European Journal of Biochemistry, 229: 1–13. doi: 10.1111/j.1432-1033.1995.0001l.x
- Issue published online: 3 MAR 2005
- Article first published online: 3 MAR 2005
- (Received 11 November 1994/6 January 1995) – EJB 94 1734/0
- transcription factors;
- protein–protein interactions;
- protein-DNA interactions;
- transcriptional regulation
The MADS-box family of transcription factors has been defined on the basis of primary sequence similarity amongst numerous proteins from a diverse range of eukaryotic organisms including yeasts, plants, insects, amphibians and mammals. The MADS-box is a conserved motif found within the DNA-binding domains of these proteins and the name refers to four of the originally identified members: MCM1, AG, DEFA and SRF. Several proteins within this family have significant biological roles. For example, the human serum-response factor (SRF) is involved in co-ordinating transcription of the proto-oncogene c-fos, whilst MCM1 is central to the transcriptional control of cell-type specific genes and the pheromone response in the yeast Saccharomyces cerevisiae. The RSRF/MEF2 proteins comprise a subfamily of this class of transcription factors which are key components in muscle-specific gene regulation. Moreover, in plants, MADS-box proteins such as AG, DEFA and GLO play fundamental roles during flower development.
The MADS-box is a contiguous conserved sequence of 56 amino acids, of which 9 are identical in all family members described so far. Several members have been shown to form dimers and consequently two functional regions within the MADS-box have been defined. The N-terminal half is the major determinant of DNA-binding specificity whilst the C-terminal half is necessary for dimerisation. This organisation allows the potential formation of numerous proteins, with subtly different DNA-binding specificities, from a limited number of genes by heterodimerisation between different MADS-box proteins. The majority of MADS-box proteins bind similar sites based on the consensus sequence CC(A/T)6 GG although each protein apparently possesses a distinct binding specificity. Moreover, several MADS-box proteins specifically recruit other transcription factors into multi-component regulatory complexes. Such interactions with other proteins appears to be a common theme within this family and play a pivotal role in the regulation of target genes.