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  Structure and assembly of the mitochondrial membrane remodelling GTPase Mgm1

Faelber, K., Dietrich, L., Noel, J. K., Wollweber, F., Pfitzner, A.-K., Mühleip, A., et al. (2019). Structure and assembly of the mitochondrial membrane remodelling GTPase Mgm1. Nature, 571(7765), 429-433. doi:10.1038/s41586-019-1372-3.

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Faelber, Katja1, Author
Dietrich, Lea2, Author           
Noel, Jeffrey K.1, Author
Wollweber, Florian3, Author
Pfitzner, Anna-Katharina4, Author
Mühleip, Alexander2, Author           
Sánchez, Ricardo5, Author           
Kudryashev, Misha5, Author                 
Chiaruttini, Nicholas4, Author
Lilie, Hauke6, Author
Schlegel, Jeanette1, Author
Rosenbaum, Eva1, Author
Hessenberger, Manuel1, Author
Matthaeus, Claudia1, Author
Kunz, Séverine7, Author
von der Malsburg, Alexander3, Author
Noè, Frank8, Author
Roux, Aurélien4, Author
van der Laan, Martin3, Author
Kühlbrandt, Werner2, Author                 
Daumke, Oliner1, 9, Author more..
1Crystallography, Max-Delbrück-Centrum for Molecular Medicine, Berlin, Germany, ou_persistent22              
2Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068291              
3Medical Biochemistry & Molecular Biology, Center for Molecular Signaling, PZMS, Saarland University Medical School, Homburg, Germany, ou_persistent22              
4Biochemistry Department, University of Geneva, Geneva, Switzerland, ou_persistent22              
5Sofja Kovalevskaja Group, Max Planck Institute of Biophysics, Max Planck Society, ou_2253651              
6Institute of Biochemistry and Biotechnology, Section of Protein Biochemistry, Martin Luther University Halle-Wittenberg, Halle (Saale), Germany, ou_persistent22              
7EM facility, Max-Delbrück-Centrum for Molecular Medicine, Berlin, Germany, ou_persistent22              
8Institute for Mathematics, Freie Universität Berlin, Berlin, Germany, ou_persistent22              
9Institute of Chemistry and Biochemistry, Freie Universität Berlin, Berlin, Germany , ou_persistent22              


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 Abstract: Balanced fusion and fission are key for the proper function and physiology of mitochondria. Remodelling of the mitochondrial inner membrane is mediated by the dynamin-like protein mitochondrial genome maintenance 1 (Mgm1) in fungi or the related protein optic atrophy 1 (OPA1) in animals. Mgm1 is required for the preservation of mitochondrial DNA in yeast, whereas mutations in the OPA1 gene in humans are a common cause of autosomal dominant optic atrophy-a genetic disorder that affects the optic nerve. Mgm1 and OPA1 are present in mitochondria as a membrane-integral long form and a short form that is soluble in the intermembrane space. Yeast strains that express temperature-sensitive mutants of Mgm1 or mammalian cells that lack OPA1 display fragmented mitochondria, which suggests that Mgm1 and OPA1 have an important role in inner-membrane fusion. Consistently, only the mitochondrial outer membrane-not the inner membrane-fuses in the absence of functional Mgm1. Mgm1 and OPA1 have also been shown to maintain proper cristae architecture; for example, OPA1 prevents the release of pro-apoptotic factors by tightening crista junctions. Finally, the short form of OPA1 localizes to mitochondrial constriction sites, where it presumably promotes mitochondrial fission. How Mgm1 and OPA1 perform their diverse functions in membrane fusion, scission and cristae organization is at present unknown. Here we present crystal and electron cryo-tomography structures of Mgm1 from Chaetomium thermophilum. Mgm1 consists of a GTPase (G) domain, a bundle signalling element domain, a stalk, and a paddle domain that contains a membrane-binding site. Biochemical and cell-based experiments demonstrate that the Mgm1 stalk mediates the assembly of bent tetramers into helical filaments. Electron cryo-tomography studies of Mgm1-decorated lipid tubes and fluorescence microscopy experiments on reconstituted membrane tubes indicate how the tetramers assemble on positively or negatively curved membranes. Our findings convey how Mgm1 and OPA1 filaments dynamically remodel the mitochondrial inner membrane.


Language(s): eng - English
 Dates: 2019-02-042019-06-132019-07-102019-07-18
 Publication Status: Issued
 Pages: 24
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1038/s41586-019-1372-3
 Degree: -



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Title: Nature
  Abbreviation : Nature
Source Genre: Journal
Publ. Info: London : Nature Publishing Group
Pages: - Volume / Issue: 571 (7765) Sequence Number: - Start / End Page: 429 - 433 Identifier: ISSN: 0028-0836
CoNE: https://pure.mpg.de/cone/journals/resource/954925427238