scholarly journals Evolution of Plant MADS Box Transcription Factors: Evidence for Shifts in Selection Associated with Early Angiosperm Diversification and Concerted Gene Duplications

2009 ◽  
Vol 26 (10) ◽  
pp. 2229-2244 ◽  
Author(s):  
H. Shan ◽  
L. Zahn ◽  
S. Guindon ◽  
P. K. Wall ◽  
H. Kong ◽  
...  
Keyword(s):  
Transcription Factors ◽  
Gene Duplications ◽  
Mads Box ◽  
Early Angiosperm ◽  
Angiosperm Diversification

The MADS-Box Family of Transcription Factors

1995 ◽  
Vol 229 (1) ◽  
pp. 1-13 ◽  
Author(s):  
Paul Shore ◽  
Andrew D. Sharrocks
Keyword(s):  
Transcription Factors ◽  
Mads Box

Analysis of the expression of the AGL17-like clade of MADS-box transcription factors in rice

2013 ◽  
Vol 13 (5-6) ◽  
pp. 160-170 ◽  
Author(s):  
Jérôme Puig ◽  
Donaldo Meynard ◽  
Giang Ngan Khong ◽  
Germain Pauluzzi ◽  
Emmanuel Guiderdoni ◽  
...  
Keyword(s):  
Transcription Factors ◽  
Mads Box

scholarly journals Activated Notch Inhibits Myogenic Activity of the MADS-Box Transcription Factor Myocyte Enhancer Factor 2C

1999 ◽  
Vol 19 (4) ◽  
pp. 2853-2862 ◽  
Author(s):  
Jeanne Wilson-Rawls ◽  
Jeffery D. Molkentin ◽  
Brian L. Black ◽  
Eric N. Olson
Keyword(s):  
Transcription Factors ◽  
Dna Binding ◽  
Notch Signaling Pathway ◽  
Mads Box ◽  
Dna Binding Domains ◽  
Muscle Gene Expression ◽  
Binding Domains ◽  
Myocyte Enhancer Factor ◽  
Bhlh Proteins ◽  
Enhancer Factor

ABSTRACT Skeletal muscle gene expression is dependent on combinatorial associations between members of the MyoD family of basic helix-loop-helix (bHLH) transcription factors and the myocyte enhancer factor 2 (MEF2) family of MADS-box transcription factors. The transmembrane receptor Notch interferes with the muscle-inducing activity of myogenic bHLH proteins, and it has been suggested that this inhibitory activity of Notch is directed at an essential cofactor that recognizes the DNA binding domains of the myogenic bHLH proteins. Given that MEF2 proteins interact with the DNA binding domains of myogenic bHLH factors to cooperatively regulate myogenesis, we investigated whether members of the MEF2 family might serve as targets for the inhibitory effects of Notch on myogenesis. We show that a constitutively activated form of Notch specifically blocks DNA binding by MEF2C, as well as its ability to cooperate with MyoD and myogenin to activate myogenesis. Responsiveness to Notch requires a 12-amino-acid region of MEF2C immediately adjacent to the DNA binding domain that is unique to this MEF2 isoform. Two-hybrid assays and coimmunoprecipitations show that this region of MEF2C interacts directly with the ankyrin repeat region of Notch. These findings reveal a novel mechanism for Notch-mediated inhibition of myogenesis and demonstrate that the Notch signaling pathway can discriminate between different members of the MEF2 family.

scholarly journals DNA binding by MADS-box transcription factors: a molecular mechanism for differential DNA bending.

1997 ◽  
Vol 17 (5) ◽  
pp. 2876-2887 ◽  
Author(s):  
A G West ◽  
P Shore ◽  
A D Sharrocks
Keyword(s):  
Transcription Factors ◽  
Dna Binding ◽  
Serum Response Factor ◽  
Dna Bending ◽  
Binding Specificity ◽  
Single Amino Acid ◽  
Specific Gene ◽  
Mads Box ◽  
Dna Binding Specificity ◽  
Single Amino Acid Residue

The serum response factor (SRF) and myocyte enhancer factor 2A (MEF2A) represent two human members of the MADS-box transcription factor family. Each protein has a distinct biological function which is reflected by the distinct specificities of the proteins for coregulatory protein partners and DNA-binding sites. In this study, we have investigated the mechanism of DNA binding utilized by these two related transcription factors. Although SRF and MEF2A belong to the same family and contain related DNA-binding domains, their DNA-binding mechanisms differ in several key aspects. In contrast to the dramatic DNA bending induced by SRF, MEF2A induces minimal DNA distortion. A combination of loss- and gain-of-function mutagenesis identified a single amino acid residue located at the N terminus of the recognition helices as the critical mediator of this differential DNA bending. This residue is also involved in determining DNA-binding specificity, thus indicating a link between DNA bending and DNA-binding specificity determination. Furthermore, different basic residues within the putative recognition alpha-helices are critical for DNA binding, and the role of the C-terminal extensions to the MADS box in dimerization between SRF and MEF2A also differs. These important differences in the molecular interactions of SRF and MEF2A are likely to contribute to their differing roles in the regulation of specific gene transcription.

scholarly journals Protein interactions of MADS box transcription factors involved in flowering in Lolium perenne

2006 ◽  
Vol 57 (13) ◽  
pp. 3419-3431 ◽  
Author(s):  
S. Ciannamea ◽  
K. Kaufmann ◽  
M. Frau ◽  
I. A. N. Tonaco ◽  
K. Petersen ◽  
...  
Keyword(s):  
Transcription Factors ◽  
Lolium Perenne ◽  
Protein Interactions ◽  
Mads Box

scholarly journals The RIN-MC Fusion of MADS-Box Transcription Factors Has Transcriptional Activity and Modulates Expression of Many Ripening Genes

2017 ◽  
Vol 176 (1) ◽  
pp. 891-909 ◽  
Author(s):  
Shan Li ◽  
Huijinlan Xu ◽  
Zheng Ju ◽  
Dongyan Cao ◽  
Hongliang Zhu ◽  
...  
Keyword(s):  
Transcription Factors ◽  
Transcriptional Activity ◽  
Mads Box ◽  
Ripening Genes
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