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  E-mail Message: I thought you might be interested in this item at http://www.worldcat.org/oclc/1226469264 Title: Gaining insights into mitochondrial membrane fusion through a structural and dynamic atomistic model of the mitofusin Fzo1p Author: Dario De Vecchis; Antoine Taly; Jérôme Hénin; Olivier Taboureau; Martin‏ Spichty; James N Sturgis, biologiste); Valérie Taly, enseignant-chercheur en biologie); Marc Baaden; Université Sorbonne Paris Cité; École doctorale Médicament, toxicologie, chimie, imageries (Paris / 2014-....); Laboratoire de biochimie théorique (Paris); Institut de biologie physico-chimique (Paris); Université Paris Diderot - Paris 7 (1970-2019) Publisher: 2017. OCLC:1226469264

  
  

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Gaining insights into mitochondrial membrane fusion through a structural and dynamic atomistic model of the mitofusin Fzo1p

Author:	Dario De Vecchis; Antoine Taly; Jérôme Hénin; Olivier Taboureau; Martin‏ Spichty; All authors
Publisher:	2017.
Dissertation:	Thèse de doctorat : Bioinformatique, Modélisation moléculaire : Sorbonne Paris Cité : 2017.
Edition/Format:	Computer file : Document : Thesis/dissertation : English
Summary:	Les mitochondries sont des organites dynamiques dont la morphologie dépend de l'équilibre fusion/fission de leurs membranes. Ce processus essentiel à la survie cellulaire est nommé dynamique mitochondriale et sa dérégulation est associée à des troubles neurologiques. Cependant les mécanismes précis régissant la dynamique mitochondriale ne sont pas élucidés. Cette thèse porte sur la protéine Fzo1p, une grande GTPase de la superfamille des Dynamin-related-Protein. C'est un élément clé impliqué dans la fusion mitochondriale de la membrane externe de la levure. Sa structure et sa dynamique ont été étudiées par modélisation et simulations de dynamiques moléculaires tout-atome dans une bicouche lipidique solvatée. Le modèle structural obtenu tient compte de données expérimentales, de template structuraux, et de modèles ab initio du domaine transmembranaire de Fzo1p. Ce modèle a été validé expérimentalement par mutagenèse dirigée. Des permutations de charges ont confirmé des ponts salins à longue distance prédits dans le modèle. En outre, des mutations ont montré que les domaines coiled-coil de Fzo1p, contrairement à sa partie N-terminale, sont indispensables à sa fonction. L'ensemble des résultats expérimentaux et in silico met en évidence l'implication des domaines charnières dans le changement conformationnel de Fzo1p, ainsi que des résidus critiques affectant sa stabilité. Les précisions atomiques obtenues sur l'interaction de Fzo1p avec le GDP permet de formuler des hypothèses sur le mécanisme moléculaire de la catalyse du GTP pour la fusion membranaire; voire à la compréhension de la dynamique mitochondriale. Mitochondria are dynamic organelles whose morphology is determined by fusion and fission of their membranes. This essential process is known as mitochondrial dynamics. Defects in mitochondrial dynamics are associated with neurological disorders making the investigation of physiological relevance. However, the precise sequence of events that lead mitochondrial dynamics are still not well characterised. Fzo1p, a large GTPase of the Dynamin-Related Proteins superfamily, is a key component in mitochondrial outer membrane fusion in yeast. During this PhD project I built a model of the protein Fzo1p. The structure and dynamics of the model was investigated through molecular modelling and all-atom molecular dynamics simulation in a fully hydrated lipid bilayer environment. The Fzo1p structural model integrates information from several template structures, experimental knowledge, as well as ab initio models of the transmembrane segments. The model is validated experimentally through directed mutagenesis, for instance charge-swap mutations confirm predicted long-distance salt bridges. A series of mutants indicate that coiled-coil domains are required for protein function at variance with its N-terminal region. Overall, the experimental and in silico approaches pinpoint the hinge domains involved in the putative conformational change and identifies critical residues affecting protein stability. Finally, key Fzo1p-GDP interactions provide insights about the molecular mechanism of membrane fusion catalysis. The model provides insight on atomic level and proposes a structure that will be instructional to understanding mitochondrial membrane fusion.  Read more...
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Subjects	Mitochondries. Bioinformatique structurale. Fusion membranaire. View all subjects
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