Abstract
Import of proteins into organelles usually requires a cis-acting targeting signal. Analysis of various hybrid proteins, consisting of mouse DHFR and parts of catalase A from Saccharomyces cerevisiae, revealed that fusion proteins containing the N-terminal 126 amino acids, or less, of catalase A remain in the cytosol whereas fusion proteins containing 140, or more, N-terminal amino acids of catalase A form large aggregates inside the cell. These protein bodies, which lack a surrounding membrane, copurified with peroxisomes on cell fractionation. The peroxisomal targeting signal of catalase A does not reside at the C-terminus or at the N-terminus.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Biological Transport
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Blotting, Western
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Catalase / chemistry
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Catalase / genetics
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Catalase / metabolism*
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Cloning, Molecular
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Gene Expression Regulation, Fungal*
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Immunohistochemistry
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Microbodies / metabolism*
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Microscopy, Electron
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Molecular Sequence Data
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Recombinant Fusion Proteins / chemistry
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Recombinant Fusion Proteins / genetics
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Recombinant Fusion Proteins / metabolism*
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Saccharomyces cerevisiae / enzymology
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Saccharomyces cerevisiae / genetics*
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Tetrahydrofolate Dehydrogenase / chemistry
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Tetrahydrofolate Dehydrogenase / genetics
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Tetrahydrofolate Dehydrogenase / metabolism*
Substances
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Recombinant Fusion Proteins
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Catalase
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Tetrahydrofolate Dehydrogenase