THE AMINO-TERMINAL REGION OF AN IMPORTED MITOCHONDRIAL PRECURSOR POLYPEPTIDE CAN DIRECT CYTOPLASMIC DIHYDROFOLATE-REDUCTASE INTO THE MITOCHONDRIAL MATRIX
THE AMINO-TERMINAL REGION OF AN IMPORTED MITOCHONDRIAL PRECURSOR POLYPEPTIDE CAN DIRECT CYTOPLASMIC DIHYDROFOLATE-REDUCTASE INTO THE MITOCHONDRIAL MATRIX
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DOI:
10.1002/j.1460-2075.1984.tb02272.x
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发表时间:
1984-01-01
期刊:
影响因子:
11.4
通讯作者:
SCHATZ, G
中科院分区:
文献类型:
--
作者:
HURT, EC;PESOLDHURT, B;SCHATZ, G
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. Gene fusion 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 2 mitochondrial membranes. A non-mitochondrial protein can be transported into the mitochondrial matrix if it is fitted with a mitochondrial targeting sequence.