Mitochondrial targeting of glutathione reductase requires a leader sequence.

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Tamura T, McMicken HW, Smith CV, Hansen TN

Mitochondrial targeting of glutathione reductase requires a leader sequence.

Biochem Biophys Res Commun. 1996 May 24;222(3):659-63. doi: 10.1006/bbrc.1996.0800.

PubMed ID

8651901 [ View in PubMed

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Abstract

Glutathione reductase (GR), which catalyzes the conversion of glutathione disulfide to glutathione, is encoded in nuclear DNA, but is active in cytoplasm and mitochondria. However, analyses of known protein and DNA sequences for human GR have not revealed a potential mitochondrial targeting signal (MTS). We generated two 5'-truncated GR clones, which resulted in omission of the N-terminal 5 or 10 amino acids, to disable a potential targeting signal, and generated two GR clones containing synthetic MTS cDNAs. Transfection of Chinese hamster ovary cells with the full length human GR cDNA or with the 5'-truncated clones increased cytosolic GR activities 6- to 14-fold, but increased mitochondrial activities less than 2-fold. In contrast, transfection with either of the GR clones containing MTS cDNAs increased GR activities in mitochondria more than 24-fold. We conclude that the existing protein and DNA sequences for human GR do not contain a MTS and that such a signal is needed for effective mitochondrial targeting.

DrugBank Data that Cites this Article

Drug Targets

Drug	Target	Kind	Organism	Pharmacological Action	Actions
Glutathione disulfide	Glutathione reductase, mitochondrial	Protein	Humans	Unknown	Substrate	Details