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Start Over Author "Nicolas Levy" Journal nature communications
5 results on '"Nicolas Levy"'

1. Production of unstable proteins through the formation of stable core complexes

Author

Nicolas Levy, Sylvia Eiler, Karine Pradeau-Aubreton, Benoit Maillot, François Stricher, and Marc Ruff

Subjects
Science
Abstract

Flexible or disordered domains often hinder the purification of proteins involved in functional interactions. Here the authors describe an approach that enables the production of stable and functional complexes of otherwise unstable proteins in quantities sufficient for structural and functional studies.

Published
2016
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2. Production of unstable proteins through the formation of stable core complexes

Author

Benoit Maillot, François Stricher, Marc Ruff, Karine Pradeau-Aubreton, Sylvia Eiler, Nicolas Levy, Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), and ruff, marc

Subjects
0301 basic medicine, Protein family, [SDV.BBM.BS] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], medicine.medical_treatment, Science, Receptors, Cytoplasmic and Nuclear, General Physics and Astronomy, Context (language use), Computational biology, Biology, Article, General Biochemistry, Genetics and Molecular Biology, Cell Line, Steroid, 03 medical and health sciences, chemistry.chemical_compound, medicine, Transcriptional regulation, Humans, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], Beta (finance), [SDV.BBM.BC] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], Multidisciplinary, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], Protein Stability, General Chemistry, 3. Good health, Integrase, 030104 developmental biology, Solubility, Biochemistry, chemistry, Nuclear receptor, Multiprotein Complexes, HIV-1, Solvents, biology.protein, DNA
Abstract

Purification of proteins that participate in large transient complexes is impeded by low amounts, heterogeneity, instability and poor solubility. To circumvent these difficulties we set up a methodology that enables the production of stable complexes for structural and functional studies. This procedure is benchmarked and applied to two challenging protein families: the human steroid nuclear receptors (SNR) and the HIV-1 pre-integration complex. In the context of transcriptional regulation studies, we produce and characterize the ligand-binding domains of the glucocorticoid nuclear receptor and the oestrogen receptor beta in complex with a TIF2 (transcriptional intermediary factor 2) domain containing the three SNR-binding motifs. In the context of retroviral integration, we demonstrate the stabilization of the HIV-1 integrase by formation of complexes with partner proteins and DNA. This procedure provides a powerful research tool for structural and functional studies of proteins participating in non-covalent macromolecular complexes., Flexible or disordered domains often hinder the purification of proteins involved in functional interactions. Here the authors describe an approach that enables the production of stable and functional complexes of otherwise unstable proteins in quantities sufficient for structural and functional studies.

Published
2016

3. Loss of MTX2 causes mandibuloacral dysplasia and links mitochondrial dysfunction to altered nuclear morphology

Author

Sahar Elouej, Karim Harhouri, Morgane Le Mao, Genevieve Baujat, Sheela Nampoothiri, Hϋlya Kayserili, Nihal Al Menabawy, Laila Selim, Arianne Llamos Paneque, Christian Kubisch, Davor Lessel, Robert Rubinsztajn, Chayki Charar, Catherine Bartoli, Coraline Airault, Jean-François Deleuze, Agnes Rötig, Peter Bauer, Catarina Pereira, Abigail Loh, Nathalie Escande-Beillard, Antoine Muchir, Lisa Martino, Yosef Gruenbaum, Song-Hua Lee, Philippe Manivet, Guy Lenaers, Bruno Reversade, Nicolas Lévy, and Annachiara De Sandre-Giovannoli

Subjects
Science
Abstract

Mandibuloacral dysplasias (MADs) are rare progeroid syndromes characterized by nuclear morphological and functional abnormalities. Here the authors report that loss of mitochondrial membrane protein MTX2 causes a progeroid MAD sharing clinical features with lamin-associated progeroid syndromes.

Published
2020
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4. Vulnerability of progeroid smooth muscle cells to biomechanical forces is mediated by MMP13

Author

Patricia R. Pitrez, Luís Estronca, Luís Miguel Monteiro, Guillem Colell, Helena Vazão, Deolinda Santinha, Karim Harhouri, Daniel Thornton, Claire Navarro, Anne-Laure Egesipe, Tânia Carvalho, Rodrigo L. Dos Santos, Nicolas Lévy, James C. Smith, João Pedro de Magalhães, Alessandro Ori, Andreia Bernardo, Annachiara De Sandre-Giovannoli, Xavier Nissan, Anna Rosell, and Lino Ferreira

Subjects
Science
Abstract

Hutchinson-Gilford Progeria Syndrome (HGPS) is a premature aging disease and smooth muscle cells are the most affected cells in HGPS individuals. Here, the authors report a microfluidics platform with HGPS induced pluripotent stem cells and show that inhibition of metalloprotease 13 may reduce smooth muscle cell loss.

Published
2020
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5. Author Correction: Loss of MTX2 causes mandibuloacral dysplasia and links mitochondrial dysfunction to altered nuclear morphology

Author

Sahar Elouej, Karim Harhouri, Morgane Le Mao, Genevieve Baujat, Sheela Nampoothiri, Hϋlya Kayserili, Nihal Al Menabawy, Laila Selim, Arianne Llamos Paneque, Christian Kubisch, Davor Lessel, Robert Rubinsztajn, Chayki Charar, Catherine Bartoli, Coraline Airault, Jean-François Deleuze, Agnes Rötig, Peter Bauer, Catarina Pereira, Abigail Loh, Nathalie Escande-Beillard, Antoine Muchir, Lisa Martino, Yosef Gruenbaum, Song-Hua Lee, Philippe Manivet, Guy Lenaers, Bruno Reversade, Nicolas Lévy, and Annachiara De Sandre-Giovannoli

Subjects
Science
Abstract

An amendment to this paper has been published and can be accessed via a link at the top of the paper.

Published
2020
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