The transcriptional repressor domain of Gli3 is intrinsically disordered
| Autor: | Kalju Vanatalu, Torben Østerlund, Kristi Laur, Jüri Jarvet, Risto Tanner, Birthe B. Kragelund, Priit Kogerman, Piret Tiigimägi, Robert Tsanev |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2013 |
| Předmět: |
musculoskeletal diseases
congenital hereditary and neonatal diseases and abnormalities Operator (biology) animal structures Recombinant Fusion Proteins Protein domain Kruppel-Like Transcription Factors Repressor lcsh:Medicine Nerve Tissue Proteins Biology Intrinsically disordered proteins DNA-binding protein Cell Line 03 medical and health sciences 0302 clinical medicine Zinc Finger Protein Gli3 Proto-Oncogene Proteins GLI3 Journal Article Humans Protein Interaction Domains and Motifs Amino Acid Sequence lcsh:Science Nuclear Magnetic Resonance Biomolecular 030304 developmental biology Genetics 0303 health sciences Multidisciplinary YY1 Research Support Non-U.S. Gov't lcsh:R Cell biology DNA-Binding Proteins Intrinsically Disordered Proteins Repressor Proteins GATAD2B Mutation embryonic structures lcsh:Q 030217 neurology & neurosurgery Research Article Protein Binding |
| Zdroj: | PLoS ONE, Vol 8, Iss 10, p e76972 (2013) Tsanev, R, Vanatalu, K, Jarvet, J, Tanner, R, Laur, K, Tiigimägi, P, Kragelund, B B, Østerlund, T & Kogerman, P 2013, ' The transcriptional repressor domain of Gli3 is intrinsically disordered ', PLoS ONE, vol. 8, no. 10, e76972 . https://doi.org/10.1371/journal.pone.0076972 PLoS ONE |
| ISSN: | 1932-6203 |
| DOI: | 10.1371/journal.pone.0076972 |
| Popis: | The transcription factor Gli3 is acting mainly as a transcriptional repressor in the Sonic hedgehog signal transduction pathway. Gli3 contains a repressor domain in its N-terminus from residue G106 to E236. In this study we have characterized the intracellular structure of the Gli3 repressor domain using a combined bioinformatics and experimental approach. According to our findings the Gli3 repressor domain while being intrinsically disordered contains predicted anchor sites for partner interactions. The obvious interaction partners to test were Ski and DNA; however, with both of these the structure of Gli3 repressor domain remained disordered. To locate residues important for the repressor function we mutated several residues within the Gli3 repressor domain. Two of these, H141A and H157N, targeting predicted helical regions, significantly decreased transcriptional repression and thus identify important functional parts of the domain. |
| Databáze: | OpenAIRE |
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