Abstract
Two isoforms of mammalian cytochrome b5, which have homologous cytosolic amino-terminal catalytic domains, are located one on endoplasmic reticulum (ER b5) the other on mitochondrial outer membranes (OM b5). A cDNA coding for the previously unknown carboxyl-terminal domain of OM b5 was cloned and a chimera between the catalytic domain of ER b5 and the carboxyl-terminal region of OM b5 was expressed in cultured mammalian cells. The chimera localized to mitochondria, indicating that the carboxyl-terminal 43 amino acids of OM b5 contain sufficient information to target the catalytic domain of ER b5 to the mitochondrial outer membrane.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Base Sequence
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Binding Sites
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Cell Line
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Chlorocebus aethiops
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Cloning, Molecular
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Cytochromes b5 / biosynthesis
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Cytochromes b5 / chemistry*
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Cytochromes b5 / metabolism*
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DNA Primers
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Endoplasmic Reticulum / metabolism
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Intracellular Membranes / metabolism*
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Kidney
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Liver / metabolism
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Mammals
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Mitochondria / metabolism*
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Molecular Sequence Data
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Polymerase Chain Reaction
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Rats
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Recombinant Fusion Proteins / biosynthesis
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Recombinant Fusion Proteins / chemistry
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Recombinant Fusion Proteins / metabolism
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Sequence Homology, Amino Acid
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Transfection
Substances
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DNA Primers
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Recombinant Fusion Proteins
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Cytochromes b5