ArticleNucleic acids research1996
Substitution of basic amino acids in the basic region stabilizes DNA binding by E12 homodimers.
Article in Nucleic acids research, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 9 citations in OpenAlex.
- Alternative splicing in the differentiation of human embryonic stem cells into cardiac precursors.PLoS computational biology · 2009Article
- Regulation of immunoglobulin gene transcription in a teleost fish: identification, expression and functional properties of E2A in the channel catfish.Immunogenetics · 2005Article
- Role of arginine residues 14 and 15 in dictating DNA binding stability and transactivation of the aryl hydrocarbon receptor/aryl hydrocarbon receptor nuclear translocator heterodimer.Gene expression · 2005Article
- STAT5-induced Id-1 transcription involves recruitment of HDAC1 and deacetylation of C/EBPbeta.The EMBO journal · 2003Article
- Regulation of the expression of cyclin-dependent kinase inhibitor p21 by E2A and Id proteins.Molecular and cellular biology · 1997Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The E2A gene encodes two alternatively spliced products, E12 and E47. The two proteins differ in their basic helix-loop-helix motifs (bHLH), responsible for DNA binding and dimerization. Although both E12 and E47 can bind to DNA as heterodimers with tissue-specific bHLH proteins, E12 binds to DNA poorly as homodimers. An inhibitory domain in E12 has previously been found to prevent E12 homodimers from binding to DNA. By measuring the dissociation rates using filter binding and electrophoretic mobility shift assays, we have shown here that the inhibitory domain interferes with DNA binding by destabilizing the DNA-protein complexes. Furthermore, we have demonstrated that substitution of basic amino acids (not other amino acids) in the DNA-binding domain of E12 can increase the intrinsic DNA-binding activity of E12 and stabilize the binding complexes, thus alleviating the repression from the inhibitory domain. This ability of basic amino acids to stabilize DNA-binding complexes may be of biological significance in the case of myogenic bHLH proteins, which all possess two more basic amino acids in their DNA binding domain than E12. To function as heterodimers with E12, the myogenic bHLH proteins may need stronger DNA binding domains.
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