Deciphering the Sox-Oct partner code by quantitative cooperativity measurements
| العنوان: | Deciphering the Sox-Oct partner code by quantitative cooperativity measurements |
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| المؤلفون: | Noel X. Li, Calista Keow Leng Ng, Prasanna R. Kolatkar, Shyam Prabhakar, Sheena Chee, Ralf Jauch |
| المساهمون: | School of Biological Sciences |
| المصدر: | Nucleic Acids Research |
| بيانات النشر: | Oxford University Press (OUP), 2012. |
| سنة النشر: | 2012 |
| مصطلحات موضوعية: | endocrine system, SOX14, genetic structures, Molecular Sequence Data, Cooperativity, Plasma protein binding, Computational biology, Biology, medicine.disease_cause, Binding, Competitive, SOX Transcription Factors, Mice, Genetics, medicine, Animals, Protein Interaction Domains and Motifs, Amino Acid Sequence, Induced pluripotent stem cell, Enhancer, Molecular Biology, Transcription factor, Mutation, urogenital system, DNA, Science::Biological sciences [DRNTU], embryonic structures, Dimerization, Octamer Transcription Factor-3, Sequence Alignment, Protein Binding |
| الوصف: | Several Sox-Oct transcription factor (TF) combinations have been shown to cooperate on diverse enhancers to determine cell fates. Here, we developed a method to quantify biochemically the Sox-Oct cooperation and assessed the pairing of the high-mobility group (HMG) domains of 11 Sox TFs with Oct4 on a series of composite DNA elements. This way, we clustered Sox proteins according to their dimerization preferences illustrating that Sox HMG domains evolved different propensities to cooperate with Oct4. Sox2, Sox14, Sox21 and Sox15 strongly cooperate on the canonical element but compete with Oct4 on a recently discovered compressed element. Sry also cooperates on the canonical element but binds additively to the compressed element. In contrast, Sox17 and Sox4 cooperate more strongly on the compressed than on the canonical element. Sox5 and Sox18 show some cooperation on both elements, whereas Sox8 and Sox9 compete on both elements. Testing rationally mutated Sox proteins combined with structural modeling highlights critical amino acids for differential Sox-Oct4 partnerships and demonstrates that the cooperativity correlates with the efficiency in producing induced pluripotent stem cells. Our results suggest selective Sox-Oct partnerships in genome regulation and provide a toolset to study protein cooperation on DNA. Published version |
| وصف الملف: | application/pdf |
| تدمد: | 1362-4962 0305-1048 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::964e9019e5c4a2a3955d09e12339b7c9Test https://doi.org/10.1093/nar/gks153Test |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....964e9019e5c4a2a3955d09e12339b7c9 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 13624962 03051048 |
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