Abstract
To examine the function of the amino-terminal presequence of rat peroxisomal 3-ketoacyl-CoA thiolase precursor, fusion proteins of various amino-terminal regions of the precursor with non-peroxisomal enzymes were expressed in cultured mammalian cells. On immunofluorescence microscopy, all constructs carrying the presequence part exhibited punctate patterns of distribution, identical with that of catalase, a peroxisomal marker. Proteins lacking all or a part of the prepiece were found in the cytosol. These results indicate that the presequence of the thiolase has sufficient information for peroxisomal targeting.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Acetyl-CoA C-Acyltransferase / genetics*
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Acetyl-CoA C-Acyltransferase / metabolism
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Amino Acid Sequence
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Animals
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CHO Cells
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Cricetinae
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Enzyme Precursors / genetics*
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Enzyme Precursors / metabolism
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Escherichia coli / enzymology
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Escherichia coli / genetics
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Fluorescent Antibody Technique
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Humans
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Microbodies / enzymology*
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Molecular Sequence Data
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Plants / enzymology
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Plants / genetics
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Plasmids
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Protein Processing, Post-Translational*
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Protein Sorting Signals / genetics*
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Protein Sorting Signals / metabolism
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Rats
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Recombinant Fusion Proteins / metabolism
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Sequence Homology, Nucleic Acid
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Tetrahydrofolate Dehydrogenase / genetics
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Tetrahydrofolate Dehydrogenase / metabolism
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Transfection
Substances
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Enzyme Precursors
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Protein Sorting Signals
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Recombinant Fusion Proteins
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Tetrahydrofolate Dehydrogenase
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Acetyl-CoA C-Acyltransferase