MDJ1P, A NOVEL CHAPERONE OF THE DNAJ FAMILY, IS INVOLVED IN MITOCHONDRIAL BIOGENESIS AND PROTEIN-FOLDING
MDJ1P, A NOVEL CHAPERONE OF THE DNAJ FAMILY, IS INVOLVED IN MITOCHONDRIAL BIOGENESIS AND PROTEIN-FOLDING
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DOI：
10.1016/0092-8674(94)90317-4
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发表时间：
1994-04-22
期刊：
影响因子：
64.5
通讯作者：
NEUPERT, W
中科院分区：
文献类型：
--
作者：
ROWLEY, N;PRIPBUUS, C;NEUPERT, W
Mdj1p是DnaJ家族的一个新成员，是一种与酿酒酵母线粒体内膜相关的热休克蛋白。MDJ1基因的破坏导致了娇小的表型，线粒体DNA的丢失，以及在37摄氏度下的活力丧失。进口的前体蛋白没有受到影响，缺乏Mdj1p，但新进口的蛋白质折叠显着受损。在升高的温度下孵育后，在缺乏Mdj1p的线粒体中，测试蛋白二氢叶酸还原酶的重折叠效率显著降低。我们的结论是，Mdj1p是一个重要的线粒体伴侣，参与新进口的蛋白质的折叠和保护蛋白质对热变性和聚集。
Mdj1p, a novel member of the DnaJ family, is a heat shock protein that is associated with the inner membrane of mitochondria of Saccharomyces cerevisiae. Disruption of the MDJ1 gene resulted in a petite phenotype, loss of mitochondrial DNA, and inviability at 37 degrees C. Import of precursor proteins was not affected by a lack of Mdj1p, but folding of newly imported proteins was markedly impaired. The efficiency of refolding of a tester protein, dihydrofolate reductase, was significantly reduced in mitochondria lacking Mdj1p after incubation at elevated temperature. We conclude that Mdj1p is an important mitochondrial chaperone that participates in the folding of newly imported proteins and in the protection of proteins against heat denaturation and aggregation.