The ATP-dependent Lon protease of Mus musculus is a DNA-binding protein that is functionally conserved between yeast and mammals
The ATP-dependent Lon protease of Mus musculus is a DNA-binding protein that is functionally conserved between yeast and mammals
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DOI：
10.1016/s0378-1119(03)00403-7
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发表时间：
2003-03-13
期刊：
影响因子：
3.5
通讯作者：
Suzuki, CK
中科院分区：
文献类型：
--
作者：
Lu, B;Liu, T;Suzuki, CK
ATP依赖性Lon蛋白酶是一种从古细菌到哺乳动物线粒体都保守的多功能酶，它不仅能降解蛋白质底物，还能结合DNA。作为了解发育过程中 Lon 功能的起点，克隆了小鼠 Lon cDNA，并在培养的哺乳动物细胞、酵母和体外对编码的蛋白质进行了表征。小鼠 Lon 与人类、酵母和细菌同源物分别显示 87%、40% 和 33% 的氨基酸相似性。在肝脏 > 心脏 > 肾脏 > 睾丸中检测到单个小鼠 Lon 转录物的表达，并且存在于早期胚胎发育过程中。内源性以及瞬时过表达的小鼠 Lon 与线粒体标记物共定位，并且根据脉冲追踪研究确定其半衰期大于 24 小时。具有酶活性的小鼠 Lon 以 ATP 依赖性方式水解 ATP 并降解蛋白质和肽底物，还特异性结合单链但不结合双链 DNA 寡核苷酸。我们认为，与富含 TG 的 DNA 序列的结合在小鼠和人类蛋白质之间是保守的。此外，小鼠 Lon 在体内替代酵母蛋白的能力证明了线粒体 Lon 功能的进化保守性。 (C) 2003 Elsevier Science B.V. 保留所有权利。
The ATP-dependent Lon protease is a multi-functional enzyme that is conserved from archae to mammalian mitochondria, which not only degrades protein substrates but also binds DNA. As a starting point toward understanding Lon function in development, the mouse Lon cDNA was cloned and the encoded protein was characterized in cultured mammalian cells, in yeast and in vitro. Mouse Lon shows 87, 40 and 33% amino acid similarity with the human, yeast and bacterial homologs, respectively. Expression of a single mouse Lon transcript is detected in liver > heart > kidney > testis and is present during early embryonic development. Endogenous as well as transiently overexpressed mouse Lon co-localize with mitochondrial markers and have half-lives greater than 24 h as determined by pulse-chase studies. Enzymatically active mouse Lon that hydrolyses ATP and degrades protein and peptide substrates in an ATP-dependent manner also specifically binds to single-stranded but not to double-stranded DNA oligonucleotides. We propose that binding to TG-rich DNA sequences has been conserved between the mouse and human proteins. In addition, the evolutionary conservation of mitochondrial Lon function is demonstrated by the ability of mouse Lon to substitute for the yeast protein in vivo. (C) 2003 Elsevier Science B.V. All rights reserved.