Fate of highly expressed proteins destined to peroxisomes in Saccharomyces cerevisiae.
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.
Hartig
A
A
Institut für Allgemeine Biochemie, Universität Wien, Austria.
Ogris
M
M
Cohen
G
G
Binder
M
M
D000595:Amino Acid Sequence; D001692:Biological Transport; D015153:Blotting, Western; D002374:Catalase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D003001:Cloning, Molecular; D015966:Gene Expression Regulation, Fungal; D007150:Immunohistochemistry; D008830:Microbodies / Q000378:metabolism*; D008854:Microscopy, Electron; D008969:Molecular Sequence Data; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000201:enzymology / Q000235:genetics*; D013762:Tetrahydrofolate Dehydrogenase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
D011993:Recombinant Fusion Proteins; D002374:Catalase; D013762:Tetrahydrofolate Dehydrogenase