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Role of the mitochondrial DnaJ homologue, Mdj1p, in the prevention of heat‐induced protein aggregation
Author(s) -
Prip-Buus Carina,
Westermann Benedikt,
Schmitt Matthias,
Langer Thomas,
Neupert Walter,
Schwarz Elisabeth
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00049-x
Subject(s) - luciferase , thermolabile , hsp70 , saccharomyces cerevisiae , mitochondrion , protein aggregation , heat shock protein , chemistry , biochemistry , microbiology and biotechnology , biophysics , biology , yeast , gene , enzyme , transfection
The role of the mitochondrial Hsp70 system in the prevention of heat‐induced protein aggregation was studied in isolated mitochondria from Saccharomyces cerevisiae . Firefly luciferase was employed as a thermolabile tester protein. After shift to 40°C a transient increase of mt‐Hsp70/luciferase complex was observed, which required functional Mdj1p and Mge1p, the mitochondrial homologues of DnaJ and GrpE. The kinetics of luciferase aggregation, however, were not influenced by mutations in either mt‐Hsp70 or Mge1p. Only the absence of Mdj1p led to enhanced protein aggregation. Thus, a central role in the transient protection against heat stress is attributed to this mitochondrial DnaJ homologue.