Arakawa H, Takiguchi M, Amaya Y, Nagata S, Hayashi H, Mori M
EMBO J. 1987 May;6(5):1361-6. doi: 10.1002/j.1460-2075.1987.tb02376.x.
The sorting of homologous proteins between two separate intracellular organelles is a major unsolved problem. 3-Oxoacyl-CoA thiolase is localized in mitochondria and peroxisomes, and provides a good system for the study on the problem. Unlike most mitochondrial matrix proteins, mitochondrial 3-oxoacyl-CoA thiolase in rats is synthesized with no transient presequence and possess information for mitochondrial targeting and import in the mature protein. Two overlapping cDNA clones contained an open reading frame encoding a polypeptide of 397 amino acid residues (predicted Mr = 41,868), a 5' untranslated sequence of 164 bp, a 3' untranslated sequence of 264 bp and a poly(A) tract. The amino acid sequence of the mitochondrial thiolase is 37% identical with that of the mature portion of rat peroxisomal 3-oxoacyl-CoA thiolase precursor. These results suggest that the two thiolases have a common origin and obtained information for targeting to respective organelles during evolution. Two portions in the mitochondrial thiolase that may serve as a mitochondrial targeting signal are presented.
在两个不同的细胞内细胞器之间对同源蛋白质进行分选是一个尚未解决的主要问题。3-氧代酰基辅酶A硫解酶定位于线粒体和过氧化物酶体中，为研究该问题提供了一个良好的系统。与大多数线粒体基质蛋白不同，大鼠线粒体3-氧代酰基辅酶A硫解酶在合成时没有短暂的前导序列，并且在成熟蛋白中具有线粒体靶向和导入的信息。两个重叠的cDNA克隆包含一个开放阅读框，编码一个由397个氨基酸残基组成的多肽（预测分子量=41,868）、一个164 bp的5'非翻译序列、一个264 bp的3'非翻译序列和一个聚腺苷酸尾。线粒体硫解酶的氨基酸序列与大鼠过氧化物酶体3-氧代酰基辅酶A硫解酶前体成熟部分的氨基酸序列有37%的同一性。这些结果表明，这两种硫解酶有共同的起源，并在进化过程中获得了靶向各自细胞器的信息。文中给出了线粒体硫解酶中可能作为线粒体靶向信号的两个部分。
