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酵母线粒体导入受体基因的分离与鉴定

Isolation and characterization of the gene for a yeast mitochondrial import receptor.

作者信息

Murakami H, Blobel G, Pain D

机构信息

Howard Hughes Medical Institute, Rockefeller University, New York, New York 10021.

出版信息

Nature. 1990 Oct 4;347(6292):488-91. doi: 10.1038/347488a0.

Abstract

We have previously identified an integral membrane protein (p32) from Saccharomyces cerevisiae as a receptor for protein import into mitochondria, and have localized it to the mitochondrial outer membrane at contact sites. Here we report isolation of the corresponding mitochondrial import receptor gene, termed MIR1. The deduced amino-acid sequence of p32 shows roughly 40% identity with proteins of bovine heart and rat liver that have been suggested to be mitochondrial phosphate carriers. Haploid cells carrying a disrupted MIR1 allele were unable to grow on a non-fermentable carbon source but grew in media containing glucose, indicating that the MIR1 protein is essential for mitochondrial function. Compared with wild type, amounts of some mitochondrial proteins were markedly reduced in cells containing a disrupted MIR1 allele, whereas levels of others were unchanged. This indicates that yeast contains more than one pathway for protein import into mitochondria.

摘要

我们之前已鉴定出酿酒酵母中的一种整合膜蛋白(p32)是蛋白质导入线粒体的受体,并将其定位到线粒体外膜的接触位点。在此,我们报告了相应的线粒体导入受体基因(称为MIR1)的分离。推导的p32氨基酸序列与牛心和大鼠肝脏中被认为是线粒体磷酸盐载体的蛋白质约有40%的同一性。携带破坏的MIR1等位基因的单倍体细胞不能在非发酵碳源上生长,但能在含葡萄糖的培养基中生长,这表明MIR1蛋白对线粒体功能至关重要。与野生型相比,含有破坏的MIR1等位基因的细胞中一些线粒体蛋白的量显著减少,而其他蛋白的水平未变。这表明酵母含有不止一条蛋白质导入线粒体的途径。

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