W Voos

Summary

Affiliation: University of Freiburg
Country: Germany

Publications

  1. ncbi Mechanisms of protein translocation into mitochondria
    W Voos
    Institut fur Biochemie und Molekularbiologie, Universitat Freiburg, Hermann Herder Str 7, D 79104, Freiburg, Germany
    Biochim Biophys Acta 1422:235-54. 1999
  2. ncbi The two mitochondrial heat shock proteins 70, Ssc1 and Ssq1, compete for the cochaperone Mge1
    S Schmidt
    Institut fur Biochemie und Molekularbiologie, Universitat Freiburg, Hermann Herder Str 7, D 79104, Germany
    J Mol Biol 313:13-26. 2001
  3. ncbi Mitochondrial import driving forces: enhanced trapping by matrix Hsp70 stimulates translocation and reduces the membrane potential dependence of loosely folded preproteins
    A Geissler
    Institut fur Biochemie und Molekularbiologie, Universitat Freiburg, D 79104 Freiburg, Germany
    Mol Cell Biol 21:7097-104. 2001
  4. ncbi Mitochondrial protein import motor: the ATPase domain of matrix Hsp70 is crucial for binding to Tim44, while the peptide binding domain and the carboxy-terminal segment play a stimulatory role
    T Krimmer
    Institut fur Biochemie und Molekularbiologie, Germany
    Mol Cell Biol 20:5879-87. 2000
  5. ncbi Presequence and mature part of preproteins strongly influence the dependence of mitochondrial protein import on heat shock protein 70 in the matrix
    W Voos
    Biochemisches Institut, Universitat Freiburg, Germany
    J Cell Biol 123:119-26. 1993
  6. ncbi Targeting and translocation of the phosphate carrier/p32 to the inner membrane of yeast mitochondria
    K Dietmeier
    Biochemisches Institut, Universitat Freiburg, Germany
    J Biol Chem 268:25958-64. 1993
  7. ncbi Differential requirement for the mitochondrial Hsp70-Tim44 complex in unfolding and translocation of preproteins
    W Voos
    Institut fur Biochemie und Molekularbiologie, Universitat Freiburg, Germany
    EMBO J 15:2668-77. 1996
  8. ncbi The J-related segment of tim44 is essential for cell viability: a mutant Tim44 remains in the mitochondrial import site, but inefficiently recruits mtHsp70 and impairs protein translocation
    A Merlin
    Institut fur Biochemie und Molekularbiologie, Universitat Freiburg, D 79104 Freiburg, Germany
    J Cell Biol 145:961-72. 1999
  9. ncbi Mitochondrial GrpE is present in a complex with hsp70 and preproteins in transit across membranes
    W Voos
    Biochemisches Institut, Universitat Freiburg, Germany
    Mol Cell Biol 14:6627-34. 1994

Collaborators

Detail Information

Publications9

  1. ncbi Mechanisms of protein translocation into mitochondria
    W Voos
    Institut fur Biochemie und Molekularbiologie, Universitat Freiburg, Hermann Herder Str 7, D 79104, Freiburg, Germany
    Biochim Biophys Acta 1422:235-54. 1999
    ....
  2. ncbi The two mitochondrial heat shock proteins 70, Ssc1 and Ssq1, compete for the cochaperone Mge1
    S Schmidt
    Institut fur Biochemie und Molekularbiologie, Universitat Freiburg, Hermann Herder Str 7, D 79104, Germany
    J Mol Biol 313:13-26. 2001
    ..We conclude that mitochondria represent the unique case where two Hsp70s compete for the interaction with one nucleotide exchange factor...
  3. ncbi Mitochondrial import driving forces: enhanced trapping by matrix Hsp70 stimulates translocation and reduces the membrane potential dependence of loosely folded preproteins
    A Geissler
    Institut fur Biochemie und Molekularbiologie, Universitat Freiburg, D 79104 Freiburg, Germany
    Mol Cell Biol 21:7097-104. 2001
    ....
  4. ncbi Mitochondrial protein import motor: the ATPase domain of matrix Hsp70 is crucial for binding to Tim44, while the peptide binding domain and the carboxy-terminal segment play a stimulatory role
    T Krimmer
    Institut fur Biochemie und Molekularbiologie, Germany
    Mol Cell Biol 20:5879-87. 2000
    ..We conclude that the ATPase domain of mtHsp70 is essential for and directly interacts with Tim44, clearly separating the mtHsp70-Tim44 interaction from the mtHsp70-substrate interaction...
  5. ncbi Presequence and mature part of preproteins strongly influence the dependence of mitochondrial protein import on heat shock protein 70 in the matrix
    W Voos
    Biochemisches Institut, Universitat Freiburg, Germany
    J Cell Biol 123:119-26. 1993
    ....
  6. ncbi Targeting and translocation of the phosphate carrier/p32 to the inner membrane of yeast mitochondria
    K Dietmeier
    Biochemisches Institut, Universitat Freiburg, Germany
    J Biol Chem 268:25958-64. 1993
    ..Yeast PiC/p32 is thus not only structurally homologous to the ADP/ATP carrier, but has a similar targeting mechanism and submitochondrial location, supporting its classification as a member of the inner membrane carrier family...
  7. ncbi Differential requirement for the mitochondrial Hsp70-Tim44 complex in unfolding and translocation of preproteins
    W Voos
    Institut fur Biochemie und Molekularbiologie, Universitat Freiburg, Germany
    EMBO J 15:2668-77. 1996
    ..This is consistent with a model that the dynamic interaction of mtHsp70 with Tim44 generates a pulling force on preproteins which supports unfolding during translocation...
  8. ncbi The J-related segment of tim44 is essential for cell viability: a mutant Tim44 remains in the mitochondrial import site, but inefficiently recruits mtHsp70 and impairs protein translocation
    A Merlin
    Institut fur Biochemie und Molekularbiologie, Universitat Freiburg, D 79104 Freiburg, Germany
    J Cell Biol 145:961-72. 1999
    ..The efficient cooperation of mtHsp70 with Tim44 facilitates the translocation of loosely folded preproteins and plays a crucial role in the import of preproteins which contain a tightly folded domain...
  9. ncbi Mitochondrial GrpE is present in a complex with hsp70 and preproteins in transit across membranes
    W Voos
    Biochemisches Institut, Universitat Freiburg, Germany
    Mol Cell Biol 14:6627-34. 1994
    ..After being imported into the matrix, the preprotein could be coprecipitated only by antibodies against mt-hsp70. We propose that mt-hsp70 and MGE cooperate in membrane translocation of preproteins...