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Autor
Abelein, Axel 1 Arsenian-Henriksson, Marie 1 Chen, Gefei 1 Fritz, Nicolas 1 Ghadessy, Farid J 1 Ilag, Leopold L 1 Johansson, Jan 1 Kaldmäe, Margit 1 Koeck, Philip J B 1 Kronqvist, Nina 1 Lama, Dilraj 1 Landreh, Michael 1 Lane, David P 1 Ng, Aik Seng 1 Nilsson, Lennart 1 Rising, Anna 1 Sabatier, Pierre 1 Sahin, Cagla 1 Saluri, Mihkel 1 Sarr, Médoune 1
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Pracoviště
Department of Anatomy Physiology and ... 1 Department of Biochemistry and Biophy... 1 Department of Biomedical Engineering ... 1 Department of Biosciences and Nutriti... 1 Department of Materials and Environme... 1 Department of Microbiology Tumor and ... 1 Department of Pharmacological and Tec... 1 Disease Intervention Technology Labor... 1 Division of Physiological Chemistry 1... 1 Masaryk Memorial Cancer Institute REC... 1 School of Natural Sciences and Health... 1 The National Medical Research Center ... 1
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Autor
Abelein, Axel 1 Arsenian-Henriksson, Marie 1 Chen, Gefei 1 Fritz, Nicolas 1 Ghadessy, Farid J 1 Ilag, Leopold L 1 Johansson, Jan 1 Kaldmäe, Margit 1 Koeck, Philip J B 1 Kronqvist, Nina 1 Lama, Dilraj 1 Landreh, Michael 1 Lane, David P 1 Ng, Aik Seng 1 Nilsson, Lennart 1 Rising, Anna 1 Sabatier, Pierre 1 Sahin, Cagla 1 Saluri, Mihkel 1 Sarr, Médoune 1
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Pracoviště
Department of Anatomy Physiology and ... 1 Department of Biochemistry and Biophy... 1 Department of Biomedical Engineering ... 1 Department of Biosciences and Nutriti... 1 Department of Materials and Environme... 1 Department of Microbiology Tumor and ... 1 Department of Pharmacological and Tec... 1 Disease Intervention Technology Labor... 1 Division of Physiological Chemistry 1... 1 Masaryk Memorial Cancer Institute REC... 1 School of Natural Sciences and Health... 1 The National Medical Research Center ... 1
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Free Medical Journals od 1995 do Před 1 rokem
Free Medical Journals od 1995 do Před 1 rokem
Elsevier Open Access Journals od 1995-01-01 do Před 1 rokem
Elsevier Open Archive Journals od 1995-01-01 do Před 1 rokem
PubMed
35290795
DOI
10.1016/j.str.2022.02.013
Knihovny.cz E-zdroje
Disordered proteins pose a major challenge to structural biology. A prominent example is the tumor suppressor p53, whose low expression levels and poor conformational stability hamper the development of cancer therapeutics. All these characteristics make it a prime example of "life on the edge of solubility." Here, we investigate whether these features can be modulated by fusing the protein to a highly soluble spider silk domain (NT∗). The chimeric protein displays highly efficient translation and is fully active in human cancer cells. Biophysical characterization reveals a compact conformation, with the disordered transactivation domain of p53 wrapped around the NT∗ domain. We conclude that interactions with NT∗ help to unblock translation of the proline-rich disordered region of p53. Expression of partially disordered cancer targets is similarly enhanced by NT∗. In summary, we demonstrate that inducing co-translational folding via a molecular "spindle and thread" mechanism unblocks protein translation in vitro.
- MeSH
- lidé MeSH
- nádorový supresorový protein p53 * metabolismus MeSH
- nádory * MeSH
- proteinové domény MeSH
- vazba proteinů MeSH
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- lidé MeSH
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- časopisecké články MeSH
- práce podpořená grantem MeSH
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Po ukončení testovacího provozu bude odkaz přesměrován adresu produkční verze portálu Medvik.