Role of the mitochondrial DnaJ homologue, Mdj1p, in the prevention of heat‐induced protein aggregation

FEBS Letters

Westermann, Benedikt¹  Prip-Buus, Carina¹  Neupert, Walter¹  Langer, Thomas¹  Schmitt, Matthias¹  Schwarz, Elisabeth¹ 

[1] Institut für Physiologische Chemie, Goegthestr. 33, 80336 München, Germany

关键词: Mitochondrial Hsp70 system;    Mdj1p;    Firefly luciferase;    Heat-induced protein aggregation;    Saccharomyces cerevisiae;    E. coli;    Escherichia coli;    Hsp;    heat shock protein;    mt-Hsp60;    mitochondrial heat shock protein of 60 kDa;    mt-Hsp70;    mitochondrial heat shock protein of 70 kDa;    PMSF;    phenyl-methylsulfonylfluoride;    PAGE;    polyacrylamide gel electrophoresis;    SDS;    sodium dodecyl sulfate;    S. cerevisiae;    Saccharomyces cerevisiae;   

DOI  :  10.1016/0014-5793(96)00049-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown