The amino-terminal region of an imported mitochondrial precursor polypeptide can direct cytoplasmic dihydrofolate reductase into the mitochondrial matrix.

Research Article20 December 1984free access The amino-terminal region of an imported mitochondrial precursor polypeptide can direct cytoplasmic dihydrofolate reductase into the mitochondrial matrix. E.C. Hurt E.C. Hurt Search for more papers by this author B. Pesold-Hurt B. Pesold-Hurt Search for more papers by this author G. Schatz G. Schatz Search for more papers by this author E.C. Hurt E.C. Hurt Search for more papers by this author B. Pesold-Hurt B. Pesold-Hurt Search for more papers by this author G. Schatz G. Schatz Search for more papers by this author Author Information E.C. Hurt, B. Pesold-Hurt and G. Schatz The EMBO Journal (1984)3:3149-3156https://doi.org/10.1002/j.1460-2075.1984.tb02272.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info Subunit IV of yeast cytochrome c oxidase is encoded by a nuclear gene, synthesized in the cytosol as a precursor with a transient amino-terminal extension of 25 amino acids, and imported into the mitochondria. By gene fusion, we have attached the amino-terminal 53 amino acids of the subunit IV precursor to the amino terminus of the mouse cytosolic enzyme dihydrofolate reductase. When the resulting fusion protein was synthesized in a transcription-translation system and then incubated with energized yeast mitochondria, it was imported into the mitochondrial matrix space and processed to a shorter form by the chelator-sensitive matrix protease. No evidence was obtained that the fusion protein became stuck across one of the two mitochondrial membranes. Thus, a non-mitochondrial protein can be transported into the mitochondrial matrix if it is fitted with a mitochondrial targeting sequence. Previous ArticleNext Article Volume 3Issue 131 December 1984In this issue RelatedDetailsLoading ...