A Model for Dimerization of the SOX Group E Transcription Factor Family
| Autor: | Shokofeh Shahangian, Jamie J. Kwan, Naveen Khan, Sarah N. Ramsook, Joyce Ni, Ana Vakiloroayaei, Logan W. Donaldson |
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| Rok vydání: | 2015 |
| Předmět: |
0301 basic medicine
Models Molecular lcsh:Medicine Gene Expression Electrophoretic Mobility Shift Assay Protein Sequencing Restriction Fragment Mapping Physical Chemistry Biochemistry 0302 clinical medicine Amino Acids lcsh:Science Promoter Regions Genetic Peptide sequence chemistry.chemical_classification Multidisciplinary Crystallography Organic Compounds Physics SOX9 Transcription Factor Condensed Matter Physics Amino acid Molecular Docking Simulation Chemistry 030220 oncology & carcinogenesis HMG-Box Domains embryonic structures Physical Sciences Crystal Structure Dimerization Hydrophobic and Hydrophilic Interactions Research Article endocrine system Stereochemistry Materials Science Material Properties Biology Research and Analysis Methods DNA-binding protein 03 medical and health sciences DNA-binding proteins Genetics Humans Solid State Physics Protein–DNA interaction Gene Regulation Amino Acid Sequence Binding site Molecular Biology Techniques Sequencing Techniques Transcription factor Molecular Biology Binding Sites Biology and life sciences lcsh:R Gene Mapping Organic Chemistry Chemical Compounds Proteins Promoter Regulatory Proteins 030104 developmental biology High-mobility group chemistry Amino Acid Substitution Chemical Properties Solubility lcsh:Q Protein Multimerization Transcription Factors |
| Zdroj: | PLoS ONE PLoS ONE, Vol 11, Iss 8, p e0161432 (2016) |
| ISSN: | 1932-6203 |
| Popis: | Group E members of the SOX transcription factor family include SOX8, SOX9, and SOX10. Preceding the high mobility group (HMG) domain in each of these proteins is a thirty-eight amino acid region that supports the formation of dimers on promoters containing tandemly inverted sites. The purpose of this study was to obtain new structural insights into how the dimerization region functions with the HMG domain. From a mutagenic scan of the dimerization region, the most essential amino acids of the dimerization region were clustered on the hydrophobic face of a single, predicted amphipathic helix. Consistent with our hypothesis that the dimerization region directly contacts the HMG domain, a peptide corresponding to the dimerization region bound a preassembled HMG-DNA complex. Sequence conservation among Group E members served as a basis to identify two surface exposed amino acids in the HMG domain of SOX9 that were necessary for dimerization. These data were combined to make a molecular model that places the dimerization region of one SOX9 protein onto the HMG domain of another SOX9 protein situated at the opposing site of a tandem promoter. The model provides a detailed foundation for assessing the impact of mutations on SOX Group E transcription factors. |
| Databáze: | OpenAIRE |
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