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Atypical Pattern of Utilization of Amino Acids for Mitochondrial Protein Synthesis in HeLa Cells

机译:HeLa细胞中利用线粒体蛋白合成氨基酸的非典型模式

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摘要

The capacity of HeLa cell mitochondria, either isolated or in intact cells, to incorporate different labeled amino acids into proteins was investigated. Eight amino acids (alanine, arginine, aspartic acid, cysteine, glutamic acid, glutamine, glycine, and lysine), which include most of the charged polar ones, showed a very low amount, if any at all, of chloramphenicol-sensitive incorporation, relative to that expected for an “average” HeLa-cell protein. By contrast, the most hydrophobic amino acids (leucine, isoleucine, valine, phenylalanine, and methionine) were the most actively incorporated by HeLa mitochondria. The available evidence suggests that pool effects cannot account for this general pattern of utilization of amino acids; furthermore, this pattern is in good agreement with the known hydrophobic properties of proteins synthesized in mitochondria.
机译:研究了分离或完整细胞中HeLa细胞线粒体将不同标记的氨基酸整合到蛋白质中的能力。八种氨基酸(丙氨酸,精氨酸,天冬氨酸,半胱氨酸,谷氨酸,谷氨酰胺,甘氨酸和赖氨酸)包括大多数带电荷的极性氨基酸,显示出非常低的氯霉素敏感性掺入量(如果有的话),相对于预期的“平均” HeLa细胞蛋白而言。相反,最疏水的氨基酸(亮氨酸,异亮氨酸,缬氨酸,苯丙氨酸和蛋氨酸)是HeLa线粒体最活跃的氨基酸。现有证据表明,池效应不能解释这种氨基酸利用的一般模式。此外,该模式与线粒体中合成的蛋白质的已知疏水特性非常吻合。

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