Wolfgang Voos

Summary

Affiliation: University of Freiburg
Country: Germany

Publications

  1. ncbi request reprint Molecular chaperones as essential mediators of mitochondrial biogenesis
    Wolfgang Voos
    Institut fur Biochemie und Molekularbiologie, Universitat Freiburg, Hermann Herder Str 7, D 79104, Freiburg, Germany
    Biochim Biophys Acta 1592:51-62. 2002
  2. pmc Proteomic analysis of mitochondrial protein turnover: identification of novel substrate proteins of the matrix protease pim1
    Tamara Major
    Institut fur Biochemie und Molekularbiologie, Universitat Freiburg, Hermann Herder Str 7, 79104 Freiburg, Germany
    Mol Cell Biol 26:762-76. 2006
  3. ncbi request reprint Pam16 has an essential role in the mitochondrial protein import motor
    Ann E Frazier
    Institut fur Biochemie und Molekularbiologie, und Fakultät für Biologie, Universitat Freiburg, D 79104 Freiburg, Germany
    Nat Struct Mol Biol 11:226-33. 2004
  4. pmc A cooperative action of the ATP-dependent import motor complex and the inner membrane potential drives mitochondrial preprotein import
    Martin Krayl
    Institut fur Biochemie und Molekularbiologie, Hermann Herder Strasse 7, D 79104 Freiburg, Germany
    Mol Cell Biol 27:411-25. 2007
  5. doi request reprint Impaired interdomain communication in mitochondrial Hsp70 results in the loss of inward-directed translocation force
    Dorothea Becker
    Institut fur Biochemie und Molekularbiologie, Universitat Bonn, Bonn, Germany
    J Biol Chem 284:2934-46. 2009
  6. pmc A J-protein is an essential subunit of the presequence translocase-associated protein import motor of mitochondria
    Kaye N Truscott
    Institut fur Biochemie und Molekularbiologie, Universitat Freiburg, D 79104 Freiburg, Germany
    J Cell Biol 163:707-13. 2003
  7. ncbi request reprint Structural properties of substrate proteins determine their proteolysis by the mitochondrial AAA+ protease Pim1
    Birgit von Janowsky
    Institut fur Biochemie und Molekularbiologie, Universitat Freiburg, Hermann Herder Str 7, D 79104 Freiburg, Germany
    Biol Chem 386:1307-17. 2005
  8. ncbi request reprint The disaggregation activity of the mitochondrial ClpB homolog Hsp78 maintains Hsp70 function during heat stress
    Birgit von Janowsky
    Institut fur Biochemie und Molekularbiologie, Hermann Herder Str 7, Universitat Freiburg, 79104 Freiburg, Germany
    J Mol Biol 357:793-807. 2006
  9. ncbi request reprint Global analysis of the mitochondrial N-proteome identifies a processing peptidase critical for protein stability
    F Nora Vögtle
    Institut fur Biochemie und Molekularbiologie, ZBMZ, Universitat Freiburg, 79104 Freiburg, Germany
    Cell 139:428-39. 2009
  10. pmc Mitochondrial translocation contact sites: separation of dynamic and stabilizing elements in formation of a TOM-TIM-preprotein supercomplex
    Agnieszka Chacinska
    Institut fur Biochemie und Molekularbiologie, Universitat Freiburg, Hermann Herder Strasse 7, D 79104 Freiburg, Germany
    EMBO J 22:5370-81. 2003

Collaborators

  • Nikolaus Pfanner
  • Peter Rehling
  • Kaye N Truscott
  • Josef Kellermann
  • Kris Gevaert
  • Axel Mogk
  • Martin Krayl
  • Dorothea Becker
  • Bernard Guiard
  • Claudia Leidhold
  • Birgit von Janowsky
  • Andreas Strub
  • Tamara Major
  • Yanfeng Li
  • Tom Bender
  • Cristina Guardia-Laguarta
  • Chris Meisinger
  • Agnieszka Chacinska
  • Ann E Frazier
  • F Nora Vögtle
  • Thomas Ruppert
  • Karin Rottgers
  • Albert Sickmann
  • Pablo Porras
  • Michael Meinecke
  • Karin Knapp
  • Jan Dudek
  • Nicole Zufall
  • Jordi Magrane
  • Serge Przedborski
  • Cornelia Rüb
  • Yuhui Liu
  • Estela Area-Gomez
  • Eric A Schon
  • Sebastian Franken
  • Rene P Zahedi
  • Matthias P Mayer
  • Stefanie Wortelkamp
  • Joo Hyun Lim
  • Falk Martin
  • Richard Wagner
  • J Antonio Bárcena
  • David U Mick
  • C Alicia Padilla
  • Klaus Paal
  • Peter Kovermann
  • Dana P Hutu
  • Helmut E Meyer
  • Michael G Cumsky
  • Maria Lind
  • Virginia Bilanchone
  • Andreas Geissler
  • Agnes Schulze-Specking

Detail Information

Publications25

  1. ncbi request reprint Molecular chaperones as essential mediators of mitochondrial biogenesis
    Wolfgang Voos
    Institut fur Biochemie und Molekularbiologie, Universitat Freiburg, Hermann Herder Str 7, D 79104, Freiburg, Germany
    Biochim Biophys Acta 1592:51-62. 2002
    ..Together, the chaperones of the mitochondrial matrix form a complex interdependent chaperone network that is essential for most reactions of mitochondrial protein biogenesis...
  2. pmc Proteomic analysis of mitochondrial protein turnover: identification of novel substrate proteins of the matrix protease pim1
    Tamara Major
    Institut fur Biochemie und Molekularbiologie, Universitat Freiburg, Hermann Herder Str 7, 79104 Freiburg, Germany
    Mol Cell Biol 26:762-76. 2006
    ..We could demonstrate that the functional integrity of the Pim1 substrate proteins, in particular, the presence of intact prosthetic groups, had a major influence on the susceptibility to proteolysis...
  3. ncbi request reprint Pam16 has an essential role in the mitochondrial protein import motor
    Ann E Frazier
    Institut fur Biochemie und Molekularbiologie, und Fakultät für Biologie, Universitat Freiburg, D 79104 Freiburg, Germany
    Nat Struct Mol Biol 11:226-33. 2004
    ..Thus, Pam16 is a newly identified type of motor subunit and is required to promote a functional PAM reaction cycle, thereby driving preprotein import into the matrix...
  4. pmc A cooperative action of the ATP-dependent import motor complex and the inner membrane potential drives mitochondrial preprotein import
    Martin Krayl
    Institut fur Biochemie und Molekularbiologie, Hermann Herder Strasse 7, D 79104 Freiburg, Germany
    Mol Cell Biol 27:411-25. 2007
    ..Polypeptide translocation and unfolding are mainly driven by the inward-directed translocation activity based on the functional cooperation of the import motor components...
  5. doi request reprint Impaired interdomain communication in mitochondrial Hsp70 results in the loss of inward-directed translocation force
    Dorothea Becker
    Institut fur Biochemie und Molekularbiologie, Universitat Bonn, Bonn, Germany
    J Biol Chem 284:2934-46. 2009
    ..We conclude that even a partial disruption of the interdomain communication in the mtHsp70 chaperone results in an almost complete breakdown of its translocation-driving properties...
  6. pmc A J-protein is an essential subunit of the presequence translocase-associated protein import motor of mitochondria
    Kaye N Truscott
    Institut fur Biochemie und Molekularbiologie, Universitat Freiburg, D 79104 Freiburg, Germany
    J Cell Biol 163:707-13. 2003
    ..We conclude that the reaction cycle of the PAM of mitochondria involves an essential J-protein...
  7. ncbi request reprint Structural properties of substrate proteins determine their proteolysis by the mitochondrial AAA+ protease Pim1
    Birgit von Janowsky
    Institut fur Biochemie und Molekularbiologie, Universitat Freiburg, Hermann Herder Str 7, D 79104 Freiburg, Germany
    Biol Chem 386:1307-17. 2005
    ..We propose that the requirement for an exposed, large, non-native protein segment, in combination with a limited unfolding capability, accounts for the selectivity of the protease Pim1 for damaged or misfolded polypeptides...
  8. ncbi request reprint The disaggregation activity of the mitochondrial ClpB homolog Hsp78 maintains Hsp70 function during heat stress
    Birgit von Janowsky
    Institut fur Biochemie und Molekularbiologie, Hermann Herder Str 7, Universitat Freiburg, 79104 Freiburg, Germany
    J Mol Biol 357:793-807. 2006
    ..We conclude that the protective role of Hsp78 in thermotolerance is mainly based on maintaining the molecular chaperone Ssc1 in a soluble and functional state...
  9. ncbi request reprint Global analysis of the mitochondrial N-proteome identifies a processing peptidase critical for protein stability
    F Nora Vögtle
    Institut fur Biochemie und Molekularbiologie, ZBMZ, Universitat Freiburg, 79104 Freiburg, Germany
    Cell 139:428-39. 2009
    ..Our results suggest that Icp55 is critical for stabilization of the mitochondrial proteome and illustrate how the N-proteome can serve as rich source for a systematic analysis of mitochondrial protein targeting, cleavage and turnover...
  10. pmc Mitochondrial translocation contact sites: separation of dynamic and stabilizing elements in formation of a TOM-TIM-preprotein supercomplex
    Agnieszka Chacinska
    Institut fur Biochemie und Molekularbiologie, Universitat Freiburg, Hermann Herder Strasse 7, D 79104 Freiburg, Germany
    EMBO J 22:5370-81. 2003
    ..Thus, Tim50 functions as a dynamic factor and the IMS domain of Tom22 represents a stabilizing element in formation of a productive translocation contact site supercomplex...
  11. ncbi request reprint In vitro analysis of the mitochondrial preprotein import machinery using recombinant precursor polypeptides
    Dorothea Becker
    Institute for Biochemistry and Molecular Biology, University of Freiburg, Freiburg, Germany
    Methods Mol Biol 457:59-83. 2008
    ..Accumulation of preproteins as membrane-spanning translocation intermediates further provides a basis for the functional and structural characterization of the active translocation machinery...
  12. doi request reprint The role of protein quality control in mitochondrial protein homeostasis under oxidative stress
    Tom Bender
    Institut fur Biochemie und Molekularbiologie, Universitat Bonn, Bonn, Germany
    Proteomics 10:1426-43. 2010
    ..As Pim1/LON expression was induced significantly under ROS treatment, we propose that this protease system performs a crucial protective function under oxidative stress conditions...
  13. ncbi request reprint The presequence translocase-associated protein import motor of mitochondria. Pam16 functions in an antagonistic manner to Pam18
    Yanfeng Li
    Institut fur Biochemie und Molekularbiologie, Universitat Freiburg, D 79104 Freiburg, Germany
    J Biol Chem 279:38047-54. 2004
    ..Pam16 represents a new type of cochaperone that controls the stimulatory effect of the J-protein Pam18 and regulates the interaction of mtHsp70 with precursor proteins during import into mitochondria...
  14. ncbi request reprint The ClpB homolog Hsp78 is required for the efficient degradation of proteins in the mitochondrial matrix
    Karin Rottgers
    Institut fur Biochemie und Molekularbiologie, Hermann Herder Strasse 7, D 79104 Freiburg, Germany
    J Biol Chem 277:45829-37. 2002
    ..We conclude that Hsp78 is a genuine component of the mitochondrial proteolysis system required for the efficient degradation of substrate proteins in the matrix...
  15. ncbi request reprint Structure and function of Hsp78, the mitochondrial ClpB homolog
    Claudia Leidhold
    Institut fur Biochemie und Molekularbiologie, Universitat Freiburg, D 79104 Freiburg, Germany
    J Struct Biol 156:149-64. 2006
    ..Hsp78 predominantly formed a trimeric complex under in vivo conditions. Hence, mitochondrial Hsp78s form a distinct subgroup of the ClpB chaperone family, exhibiting specific structural and functional properties...
  16. doi request reprint Mitochondrial protein homeostasis: the cooperative roles of chaperones and proteases
    Wolfgang Voos
    Institut fur Biochemie und Molekularbiologie, Universitat Bonn, Nussallee 11, 53115 Bonn, Germany
    Res Microbiol 160:718-25. 2009
    ..The coordinated biochemical activities of both Hsp78 and Pim1/LON prevent the accumulation of toxic protein aggregates in mitochondria and thereby indirectly ensure survival of the eukaryotic cell...
  17. ncbi request reprint Fluorescence-mediated analysis of mitochondrial preprotein import in vitro
    Martin Krayl
    Institut fur Biochemie und Molekularbiologie, Universitat Freiburg, D 79104 Freiburg, Germany
    Anal Biochem 355:81-9. 2006
    ..In summary, the use of a reporter domain modified with a fluorescent dye provides a novel, sensitive, and fast detection method to analyze the properties of the mitochondrial import reaction in vitro...
  18. ncbi request reprint A new connection: chaperones meet a mitochondrial receptor
    Wolfgang Voos
    Institut fur Biochemie und Molekularbiologie, Universitat Freiburg, Hermann Herder Str 7, D 79104 Freiburg, Germany
    Mol Cell 11:1-3. 2003
    ..2003) extend the function of chaperones by demonstrating that Hsp90 and Hsp70 specifically interact with the mitochondrial protein import receptor Tom70 at the outer membrane and are required for translocation of precursor proteins...
  19. ncbi request reprint The putative helical lid of the Hsp70 peptide-binding domain is required for efficient preprotein translocation into mitochondria
    Andreas Strub
    Institut fur Biochemie und Molekularbiologie, Universitat Freiburg, Hermann Herder Str 7, D 79104 Freiburg, Germany
    J Mol Biol 334:1087-99. 2003
    ..We conclude that the carboxy-terminal domain performs a crucial role in the import process by enhancing the import motor function of Ssc1 during polypeptide translocation...
  20. pmc The Hsp70 peptide-binding domain determines the interaction of the ATPase domain with Tim44 in mitochondria
    Andreas Strub
    Institut fur Biochemie und Molekularbiologie, Hermann Herder Strasse 7, D 79104 Freiburg, Germany
    EMBO J 21:2626-35. 2002
    ..Hence, the determination of a crucial Hsp70 function via the peptide-binding domain suggests a new regulatory principle for Hsp70 domain cooperation...
  21. ncbi request reprint Chaperones and proteases--guardians of protein integrity in eukaryotic organelles
    Claudia Leidhold
    Institut fur Biochemie und Molekularbiologie, Universitat Freiburg, Hermann Herder Str 7, D 79104 Freiburg, Germany
    Ann N Y Acad Sci 1113:72-86. 2007
    ..Here we present and discuss recent experimental insights into the molecular mechanisms underlying organellar PQC processes...
  22. pmc α-Synuclein is localized to mitochondria-associated ER membranes
    Cristina Guardia-Laguarta
    Departments of Pathology, Neurology, and Genetics and Development, and Center for Motor Neuron Biology and Disease, Columbia University Medical Center, New York, New York 10032, Institut fur Biochemie und Molekularbiologie, Universität 53115 Bonn, Germany, and Department of Neurology and Neuroscience, Weill Cornell Medical College, New York, New York 10065
    J Neurosci 34:249-59. 2014
    ..We believe that our results have far-reaching implications for both our understanding of α-syn biology and the treatment of synucleinopathies. ..
  23. ncbi request reprint Tim50 maintains the permeability barrier of the mitochondrial inner membrane
    Michael Meinecke
    Biophysik, Universitat Osnabruck, FB Biologie Chemie, D 49034 Osnabrück, Germany
    Science 312:1523-6. 2006
    ..Thus, the hydrophilic cis domain of Tim50 maintains the permeability barrier of mitochondria by closing the translocation pore in a presequence-regulated manner...
  24. ncbi request reprint One single in-frame AUG codon is responsible for a diversity of subcellular localizations of glutaredoxin 2 in Saccharomyces cerevisiae
    Pablo Porras
    Department of Biochemistry and Molecular Biology, University of Cordoba, 14071 Cordoba, Spain
    J Biol Chem 281:16551-62. 2006
    ..The "A" denotes adenine, rather than alanine, and the "G" refers to guanine, not glycine [corrected]..
  25. ncbi request reprint Tom40: more than just a channel
    Wolfgang Voos
    Nat Struct Biol 10:981-2. 2003