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Nils Wiedemann  - - - 
Top co-authors See all
Paul Schanda

63 shared publications

CEA; CNRS; Universite J. Fourier; Institut de Biologie Structurale; 6, rue Jules Horowitz 38000 Grenoble FRANCE

Nikolaus Pfanner

53 shared publications

Institute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg, 79104 Freiburg, Germany

Stefan Günther

25 shared publications

Institute of Pharmaceutical SciencesAlbert-Ludwigs-Universität Freiburg Hermann-Herder-Str. 9 79104 Freiburg Germany

Bettina Warscheid

19 shared publications

Faculty of Biology, Institute of Biology II, Biochemistry-Functional Proteomics, University of Freiburg, Schänzlestrasse 1, 79104, Freiburg, Germany.

Bernd Kammerer

7 shared publications

BIOSS Centre for Biological Signalling Studies, University of Freiburg, 79104 Freiburg, Germany

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Publication Record
Distribution of Articles published per year 
(2011 - 2018)
Total number of journals
published in
 
9
 
Publications See all
Article 0 Reads 0 Citations Structural Basis of Membrane Protein Chaperoning through the Mitochondrial Intermembrane Space. Katharina Weinhäupl, Caroline Lindau, Audrey Hessel, Yong Wa... Published: 15 November 2018
Cell,
PubMed View at PubMed ABS Show/hide abstract
The exchange of metabolites between the mitochondrial matrix and the cytosol depends on β-barrel channels in the outer membrane and α-helical carrier proteins in the inner membrane. The essential translocase of the inner membrane (TIM) chaperones escort these proteins through the intermembrane space, but the structural and mechanistic details remain elusive. We have used an integrated structural biology approach to reveal the functional principle of TIM chaperones. Multiple clamp-like binding sites hold the mitochondrial membrane proteins in a translocation-competent elongated form, thus mimicking characteristics of co-translational membrane insertion. The bound preprotein undergoes conformational dynamics within the chaperone binding clefts, pointing to a multitude of dynamic local binding events. Mutations in these binding sites cause cell death or growth defects associated with impairment of carrier and β-barrel protein biogenesis. Our work reveals how a single mitochondrial "transfer-chaperone" system is able to guide α-helical and β-barrel membrane proteins in a "nascent chain-like" conformation through a ribosome-free compartment.
Article 0 Reads 0 Citations Structural Basis of Membrane Protein Chaperoning through the Mitochondrial Intermembrane Space Katharina Weinhäupl, Caroline Lindau, Audrey Hessel, Yong Wa... Published: 01 November 2018
Cell, doi: 10.1016/j.cell.2018.10.039
DOI See at publisher website ABS Show/hide abstract
The exchange of metabolites between the mitochondrial matrix and the cytosol depends on β-barrel channels in the outer membrane and α-helical carrier proteins in the inner membrane. The essential translocase of the inner membrane (TIM) chaperones escort these proteins through the intermembrane space, but the structural and mechanistic details remain elusive. We have used an integrated structural biology approach to reveal the functional principle of TIM chaperones. Multiple clamp-like binding sites hold the mitochondrial membrane proteins in a translocation-competent elongated form, thus mimicking characteristics of co-translational membrane insertion. The bound preprotein undergoes conformational dynamics within the chaperone binding clefts, pointing to a multitude of dynamic local binding events. Mutations in these binding sites cause cell death or growth defects associated with impairment of carrier and β-barrel protein biogenesis. Our work reveals how a single mitochondrial "transfer-chaperone" system is able to guide α-helical and β-barrel membrane proteins in a "nascent chain-like" conformation through a ribosome-free compartment.
Article 4 Reads 5 Citations Membrane protein insertion through a mitochondrial β-barrel gate Alexandra I. C. Höhr, Caroline Lindau, Christophe Wirth, Jia... Published: 18 January 2018
Science, doi: 10.1126/science.aah6834
DOI See at publisher website PubMed View at PubMed
Conference 21 Reads 0 Citations Mitochondrial metabolomics reveals compartment-specific metabolic responses in yeast cells Daqiang Pan, Caroline Lindau, Simon Lagies, Stefan Günther, ... Published: 20 November 2017
The 2nd International Electronic Conference on Metabolomics, doi: 10.3390/iecm-2-04981
DOI See at publisher website
Article 2 Reads 45 Citations Mitochondrial Machineries for Protein Import and Assembly Nils Wiedemann, Nikolaus Pfanner Published: 20 June 2017
Annual Review of Biochemistry, doi: 10.1146/annurev-biochem-060815-014352
DOI See at publisher website PubMed View at PubMed ABS Show/hide abstract
Mitochondria are essential organelles with numerous functions in cellular metabolism and homeostasis. Most of the >1,000 different mitochondrial proteins are synthesized as precursors in the cytosol and are imported into mitochondria by five transport pathways. The protein import machineries of the mitochondrial membranes and aqueous compartments reveal a remarkable variability of mechanisms for protein recognition, translocation, and sorting. The protein translocases do not operate as separate entities but are connected to each other and to machineries with functions in energetics, membrane organization, and quality control. Here, we discuss the versatility and dynamic organization of the mitochondrial protein import machineries. Elucidating the molecular mechanisms of mitochondrial protein translocation is crucial for understanding the integration of protein translocases into a large network that controls organelle biogenesis, function, and dynamics. Expected final online publication date for the Annual Review of Biochemistry Volume 86 is June 20, 2017. Please see http://www.annualreviews.org/page/journal/pubdates for revised estimates.
Article 0 Reads 23 Citations Definition of a High-Confidence Mitochondrial Proteome at Quantitative Scale Marcel Morgenstern, Sebastian B. Stiller, Philipp Lübbert, C... Published: 01 June 2017
Cell Reports, doi: 10.1016/j.celrep.2017.06.014
DOI See at publisher website PubMed View at PubMed ABS Show/hide abstract
Mitochondria perform central functions in cellular bioenergetics, metabolism, and signaling, and their dysfunction has been linked to numerous diseases. The available studies cover only part of the mitochondrial proteome, and a separation of core mitochondrial proteins from associated fractions has not been achieved. We developed an integrative experimental approach to define the proteome of yeast mitochondria. We classified > 3,300 proteins of mitochondria and mitochondria-associated fractions and defined 901 high-confidence mitochondrial proteins, expanding the set of mitochondrial proteins by 82. Our analysis includes protein abundance under fermentable and nonfermentable growth, submitochondrial localization, single-protein experiments, and subcellular classification of mitochondria-associated fractions. We identified mitochondrial interactors of respiratory chain supercomplexes, ATP synthase, AAA proteases, the mitochondrial contact site and cristae organizing system (MICOS), and the coenzyme Q biosynthesis cluster, as well as mitochondrial proteins with dual cellular localization. The integrative proteome provides a high-confidence source for the characterization of physiological and pathophysiological functions of mitochondria and their integration into the cellular environment.
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