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Systèmes Complexes et Phénomènes Nonlinéaires
(31) Production(s) de l'année 2016
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Traffic models for the self-organizing cytoplasm
Auteur(s): Parmeggiani A.
(Séminaires)
Institut de Biologie Computationelle - Université de Montpellier (Montpellier, FR), 2016-07-13 |
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Regulating matter concentration in the cytoplasm: a modeling view from exclusion processes
Auteur(s): Parmeggiani A.
Conférence invité: CECAM Workshop "Mesoscopic Modeling in Physics of Molecular and Cell Biology” (Toulouse, FR, 2016-10-10)
Résumé: Description of recent theoretical research in the study of self-organization of cytoplasmic matter via cytoskeletal transport
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Motors, theory and other stuffs!
Some steps between physics and biology
Auteur(s): Parmeggiani A.
Conférence invité: 20 years of Physico-Chimie Curie (Paris, FR, 2016-11-10)
Résumé: Ideas in theoretical physics of biological systems
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Physical modeling of active bacterial DNA segregation
Auteur(s): Walter J.-C.
Conference: Biophychrom16: The Biology and Physics of Bacterial Chromosome Organisation (Paris, Collège de France, FR, 2016-09-15)
Texte intégral en Openaccess :
Ref HAL: hal-01931243_v1
Exporter : BibTex | endNote
Résumé: Genome processing relies on the intracellular localization and dynamic assembly of higher-order nucleoprotein complexes. In bacteria, the mechanism of assembly for the most widespread partition systems, ParABS, responsible for active DNA segregation remains elusive. We have combined super-resolution, genome-wide, biochemical and modeling approaches to investigate quantitatively the formation of the nucleoprotein complex organized around the centromere-like sequences, parS. We found that the active confinement of nearly all ParB proteins around parS, observed at the single molecule resolution, relies on a network of synergistic interactions involving protein-protein and protein-DNA interactions. Our physico-mathematical modeling of ParB binding pattern revealed that ParB binds stochastically in the vicinity of parS over long distances. Based on our findings, and consistent with previous data, we propose a new model that relies on a nucleation and looping mechanism leading to the formation of a dynamic lattice for the partition complex assembly. We thus provide new bases to model the DNA segregation process. Our original assembly model may also apply to many unrelated proteins that self-assemble in superstructures through nucleation centers.
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Voltage-Activated Ion Transport through Single-Walled Carbon Nanotubes
Auteur(s): Yazda K., Michel T., Tahir S., Picaud Fabien, Loubet Bastien, Manghi Manoel, Palmeri J., Henn F., Jourdain V.
Conference: MRS Fall Meeting (Boston, US, 2016-11-28)
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Physical modeling of active bacterial DNA segregation
Auteur(s): Walter J.-C.
Conférence invité: iPoLS Network Annual Meeting (Harvard, US, 2016-07-24)
Texte intégral en Openaccess :
Ref HAL: hal-01881332_v1
Exporter : BibTex | endNote
Résumé: Genome processing relies on the intracellular localization and dynamic assembly of higher-order nucleoprotein complexes. In bacteria, the mechanism of assembly for the most widespread partition systems, ParABS, responsible for active DNA segregation remains elusive. We have combined super-resolution, genome-wide, biochemical and modeling approaches to investigate quantitatively the formation of the nucleoprotein complex organized around the centromere-like sequences, parS. We found that the active confinement of nearly all ParB proteins around parS, observed at the single molecule resolution, relies on a network of synergistic interactions involving protein-protein and protein-DNA interactions. Our physico-mathematical modeling of ParB binding pattern revealed that ParB binds stochastically in the vicinity of parS over long distances. Based on our findings, and consistent with previous data, we propose a new model that relies on a nucleation and looping mechanism leading to the formation of a dynamic lattice for the partition complex assembly. We thus provide new bases to model the DNA segregation process. Our original assembly model may also apply to many unrelated proteins that self-assemble in superstructures through nucleation centers.
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Physical modeling of active bacterial DNA segregation
Auteur(s): Walter J.-C.
Conférence invité: Mesoscopic Modeling in Physics of Molecular and Cell Biology (Toulouse, FR, 2016-10-10)
Texte intégral en Openaccess :
Ref HAL: hal-01881271_v1
Exporter : BibTex | endNote
Résumé: Genome processing relies on the intracellular localization and dynamic assembly of higher-order nucleoprotein complexes. In bacteria, the mechanism of assembly for the most widespread partition systems, ParABS, responsible for active DNA segregation remains elusive. We have combined super-resolution, genome-wide, biochemical and modeling approaches to investigate quantitatively the formation of the nucleoprotein complex organized around the centromere-like sequences, parS. We found that the active confinement of nearly all ParB proteins around parS, observed at the single molecule resolution, relies on a network of synergistic interactions involving protein-protein and protein-DNA interactions. Our physico-mathematical modeling of ParB binding pattern revealed that ParB binds stochastically in the vicinity of parS over long distances. Based on our findings, and consistent with previous data, we propose a new model that relies on a nucleation and looping mechanism leading to the formation of a dynamic lattice for the partition complex assembly. We thus provide new bases to model the DNA segregation process. Our original assembly model may also apply to many unrelated proteins that self-assemble in superstructures through nucleation centers.
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