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

被引：40

作者：

PripBuus, C ^{[1
]}

Westermann, B ^{[1
]}

Schmitt, M ^{[1
]}

Langer, T ^{[1
]}

Neupert, W ^{[1
]}

Schwarz, E ^{[1
]}

机构：

[1] UNIV MUNICH,INST PHYSIOL CHEM,D-80336 MUNICH,GERMANY

来源：

FEBS LETTERS | 1996年 / 380卷 / 1-2期

关键词：

mitochondrial Hsp70 system; Mdj1p; firefly luciferase; heat-induced protein aggregation; Saccharomyces cerevisiae;

D O I：

10.1016/0014-5793(96)00049-X

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

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 degrees C a transient increase of mt-Hsp70 nuciferase 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.

引用

页码：142 / 146

页数：5

共 23 条

[1] A MITOCHONDRIAL HOMOLOG OF BACTERIAL GRPE INTERACTS WITH MITOCHONDRIAL HSP70 AND IS ESSENTIAL FOR VIABILITY [J].