ArticleNucleic acids research2003
Molecular determinants of the cell-cycle regulated Mcm1p-Fkh2p transcription factor complex.
Article in Nucleic acids research, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 35 citations in OpenAlex.
- Cyclin/Forkhead-mediated coordination of cyclin waves: an autonomous oscillator rationalizing the quantitative model of Cdk control for budding yeast.NPJ systems biology and applications · 2021Review
- Identification of Fkh1 and Fkh2 binding site variants associated with dynamically bound DNA elements including replication origins.Nucleus (Austin, Tex.) · 2017Article
- Binding of the Fkh1 Forkhead Associated Domain to a Phosphopeptide within the Mph1 DNA Helicase Regulates Mating-Type Switching in Budding Yeast.PLoS genetics · 2016Article
- Cell cycle regulated transcription: from yeast to cancer.F1000Research · 2016Review
- STUbL-mediated degradation of the transcription factor MATα2 requires degradation elements that coincide with corepressor binding sites.Molecular biology of the cell · 2015Article
- Fkh1 and Fkh2 bind multiple chromosomal elements in the S. cerevisiae genome with distinct specificities and cell cycle dynamics.PloS one · 2014Article
- Review
- Bck2 acts through the MADS box protein Mcm1 to activate cell-cycle-regulated genes in budding yeast.PLoS genetics · 2013Article
- A novel ab initio identification system of transcriptional regulation motifs in genome DNA sequences based on direct comparison scheme of signal/noise distributions.Nucleic acids research · 2012Article
- Forkhead transcription factors establish origin timing and long-range clustering in S. cerevisiae.Cell · 2012Article
- A competitive transcription factor binding mechanism determines the timing of late cell cycle-dependent gene expression.Molecular cell · 2010Article
- Coupling phosphate homeostasis to cell cycle-specific transcription: mitotic activation of Saccharomyces cerevisiae PHO5 by Mcm1 and Forkhead proteins.Molecular and cellular biology · 2009Article
- Precise regulation of gene expression dynamics favors complex promoter architectures.PLoS computational biology · 2009Article
- Computational detection of significant variation in binding affinity across two sets of sequences with application to the analysis of replication origins in yeast.BMC bioinformatics · 2008Article
- Forkhead proteins control the outcome of transcription factor binding by antiactivation.The EMBO journal · 2007Article
- WebMOTIFS: automated discovery, filtering and scoring of DNA sequence motifs using multiple programs and Bayesian approaches.Nucleic acids research · 2007Article
- The Isw2 chromatin-remodeling ATPase cooperates with the Fkh2 transcription factor to repress transcription of the B-type cyclin gene CLB2.Molecular and cellular biology · 2007Article
- Functional interactions between the Forkhead transcription factor FOXK1 and the MADS-box protein SRF.Nucleic acids research · 2007Article
- Clustering of genes into regulons using integrated modeling-COGRIM.Genome biology · 2007Article
- Explicit equilibrium modeling of transcription-factor binding and gene regulation.Genome biology · 2005Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
The MADS-box transcription factor Mcm1p and forkhead (FKH) transcription factor Fkh2p act in a DNA-bound complex to regulate cell-cycle dependent expression of the CLB2 cluster in Saccharomyces cerevisiae. Binding of Fkh2p requires prior binding by Mcm1p. Here we have investigated the molecular determinants governing the formation of the Mcm1p- Fkh2p complex. Fkh2p exhibits cooperativity in complex formation with Mcm1p and we have mapped a small region of Fkh2p located immediately upstream of the FKH DNA binding domain that is required for this cooperativity. This region is lacking in the related protein Fkh1p that cannot form ternary complexes with Mcm1p. A second region is identified that inhibits Mcm1p-independent DNA binding by Fkh2p. The spacing between the Mcm1p and Fkh2p binding sites is also a critical determinant for complex formation. We also show that Fkh2p can form ternary complexes with the human counterpart of Mcm1p, serum response factor (SRF). Mutations at analogous positions in Mcm1p, which are known to affect SRF interaction with its partner protein Elk-1, abrogate complex formation with Fkh2p, demonstrating evolutionary conservation of coregulatory protein binding surfaces. Our data therefore provide molecular insights into the mechanisms of Mcm1p- Fkh2p complex formation and more generally aid our understanding of MADS-box protein function.
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