ArticleBiochemistry2005
Assembly of b/HLH/z proteins c-Myc, Max, and Mad1 with cognate DNA: importance of protein-protein and protein-DNA interactions.
Article in Biochemistry, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 50 citations in OpenAlex.
- Site-Specific Acetylation of the Transcription Factor Protein Max Modulates Its DNA Binding Activity.ACS central science · 2024Article
- NMR-identification of the interaction between BRCA1 and the intrinsically disordered monomer of the Myc-associated factor X.Protein science : a publication of the Protein Society · 2024Article
- Enabling Peptide Ligation at Aromatic Junction Mimics via Native Chemical Ligation and Palladium-Mediated S-Arylation.Organic letters · 2023Article
- Review
- Targeting MYC with modular synthetic transcriptional repressors derived from bHLH DNA-binding domains.Nature biotechnology · 2023Article
- Biophysical and Structural Methods to Study the bHLHZip Region of Human c-MYC.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Structural and Biophysical Insights into the Function of the Intrinsically Disordered Myc Oncoprotein.Cells · 2020Review
- Omomyc Reveals New Mechanisms To Inhibit the MYC Oncogene.Molecular and cellular biology · 2019Article
- The structure of INI1/hSNF5 RPT1 and its interactions with the c-MYC:MAX heterodimer provide insights into the interplay between MYC and the SWI/SNF chromatin remodeling complex.The FEBS journal · 2018Article
- AR-PDEF pathway promotes tumour proliferation and upregulates MYC-mediated gene transcription by promoting MAD1 degradation in ER-negative breast cancer.Molecular cancer · 2018Article
- Synthetic molecules for disruption of the MYC protein-protein interface.Bioorganic & medicinal chemistry · 2018Article
- Direct HPV E6/Myc interactions induce histone modifications, Pol II phosphorylation, and hTERT promoter activation.Oncotarget · 2017Article
- Article
- Small-molecule inhibitors of the Myc oncoprotein.Biochimica et biophysica acta · 2015Review
- Article
- Features of protein-protein interactions that translate into potent inhibitors: topology, surface area and affinity.Expert reviews in molecular medicine · 2012Review
- MYC on the path to cancer.Cell · 2012Review
- Reengineering natural design by rational design and in vivo library selection: the HLH subdomain in bHLHZ proteins is a unique requirement for DNA-binding function.Protein engineering, design & selection : PEDS · 2010Article
- Kinetic analysis of the interaction of b/HLH/Z transcription factors Myc, Max, and Mad with cognate DNA.Biochemistry · 2010Article
- Max-E47, a designed minimalist protein that targets the E-box DNA site in vivo and in vitro.Journal of the American Chemical Society · 2009Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Among the best characterized of the transcription factors are the b/HLH/z proteins: USF, Max, Myc, and Mad. These proteins bind to the DNA E-box, a six base pair sequence, CACGTG. Max and Myc form a heterodimer that has strong oncogenic potential but can also repress transcription, while Mad and Max form a heterodimer that acts as a transcription repressor. We have used fluorescence anisotropy to measure protein-protein and protein-DNA affinity. The specific binding between MLP DNA and Max (K = 2.2 +/- 0.5 nM) is about 10-fold higher affinity than LCR DNA and about 100-fold higher than for a nonspecific DNA. USF has a similar binding affinity as Max to MLP DNA (K = 15 +/- 10 nM), but Max binds more tightly to LCR and nonspecific DNA. A series of oligonucleotides designated E-box, half-E-box, and non-E-box were constructed to examine the effects of DNA sequence. The binding results indicate that for Max protein most of the binding energy can be attributed to individual elements with little cooperativity among the two halves of the E-box. Further studies measured the equilibria for the entire thermodynamic cycle of monomer-dimer-DNA interactions. Surprisingly, the affinity of the Max monomer-DNA for the second monomer was greatly reduced (K for the first monomer in the nanomolar range and for the second monomer in the micromolar range). Looked at from the perspective of the Max protein, the binding of DNA to Max significantly reduces the affinity of the Max protein for the second monomer, whether the second monomer is Myc, Mad, or Max. These data suggest the importance of protein-protein interactions in assembly of a transcription initiation complex.
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Registered trials
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