N 端序列指导线粒体丙氨酸转氨酶导入线粒体。
The N-terminal sequence directs import of mitochondrial alanine aminotransferase into mitochondria.
作者信息
Metón Isidoro, Egea Miriam, Fernández Felipe, Eraso María C, Baanante Isabel V
机构信息
Departament de Bioquímica i Biologia Molecular, Facultat de Farmàcia, Universitat de Barcelona, Diagonal 643, 08028 Barcelona, Spain.
出版信息
FEBS Lett. 2004 May 21;566(1-3):251-4. doi: 10.1016/j.febslet.2004.04.051.
Herein, we report cloning and subcellular localization of two alanine aminotransferase (ALT) isozymes, cALT and mALT, from liver of gilthead sea bream (Sparus aurata). CHO cells transfected with constructs expressing cALT or mALT as C- or N-terminal fusion with the enhanced green fluorescent protein (EGFP) showed that cALT is cytosolic, whereas mALT localized to mitochondria. Fusion of EGFP to mALT N-terminus or removal of amino acids 1-83 of mALT avoided import into mitochondria, supporting evidence that the mALT N-terminus contains a mitochondrial targeting signal. The amino acid sequence of mALT is the first reported for a mitochondrial ALT in animals.
在此，我们报告了从金头鲷（Sparus aurata）肝脏中克隆出两种丙氨酸转氨酶（ALT）同工酶cALT和mALT及其亚细胞定位。用表达cALT或mALT并与增强型绿色荧光蛋白（EGFP）融合的C端或N端构建体转染的CHO细胞表明，cALT定位于细胞质，而mALT定位于线粒体。将EGFP融合到mALT的N端或去除mALT的1-83位氨基酸可避免其导入线粒体，这支持了mALT的N端包含线粒体靶向信号的证据。mALT的氨基酸序列是动物中线粒体ALT的首次报道。
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