Why the c‐Fos/c‐Jun complex is extremely conserved: An in vitro evolution exploration by combining cDNA display and proximity ligation
| Autor: | Bai-Xue Chen, Tian Tian, Xin-Yi Chu, Hong-Yu Zhang, Shou-Kai Kang, Pengfei Dong |
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| Rok vydání: | 2019 |
| Předmět: |
DNA
Complementary Transcription Genetic Proto-Oncogene Proteins c-jun Mutant Biophysics Biochemistry Evolution Molecular Mice 03 medical and health sciences chemistry.chemical_compound Structural Biology Complementary DNA Genetics Transcriptional regulation Animals Promoter Regions Genetic Molecular Biology Transcription factor 030304 developmental biology 0303 health sciences Polymorphism Genetic 030302 biochemistry & molecular biology c-jun DNA Sequence Analysis DNA Cell Biology Cell biology Genetic Techniques chemistry Multiprotein Complexes Mutation Protein Multimerization Ligation Proto-Oncogene Proteins c-fos Systematic evolution of ligands by exponential enrichment Protein Binding Transcription Factors |
| Zdroj: | FEBS Letters. 593:1040-1049 |
| ISSN: | 1873-3468 0014-5793 |
| DOI: | 10.1002/1873-3468.13388 |
| Popis: | Transcriptional regulation involves a series of sophisticated protein-protein and protein-DNA interactions (PPI and PDI). Some transcriptional complexes, such as c-Fos/c-Jun and their binding DNA fragments, have been conserved over the past one billion years. Considering the thermodynamic principle for transcriptional complex formation, we hypothesized that the c-Fos/c-Jun complex may represent a thermodynamic summit in the evolutionary space. To test this, we invented a new method, termed One-Pot-seq, which combines cDNA display and proximity ligation to analyse PPI/PDI complexes simultaneously. We found that the wild-type c-Fos/c-Jun complex is indeed the most thermodynamically stable relative to various mutants of c-Fos/c-Jun and binding DNA fragments. Our method also provides a universal approach to detect transcriptional complexes and explore transcriptional regulation mechanisms. |
| Databáze: | OpenAIRE |
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