Abstract
Peroxisomes are capable of importing folded and oligomeric proteins. However, it is a matter of dispute whether oligomer import by peroxisomes is the exception or the rule. Here, I argue for a clear distinction between homo-oligomeric proteins that are essentially peroxisomal, and dually localized hetero-oligomers that access the peroxisome by piggyback import, localizing there in limited number, whereas the majority remain in the cytosol. Homo-oligomeric proteins comprise the majority of all peroxisomal matrix proteins. There is evidence that binding by Pex5 in the cytosol can regulate their oligomerization state before import. The hetero-oligomer group is made up of superoxide dismutase and lactate dehydrogenase. These proteins have evolved mechanisms that render import inefficient and retain the majority of proteins in the cytosol.
Highlights
Peroxisomes are capable of importing folded and oligomeric proteins
I argue for a clear distinction between homo-oligomeric proteins that are essentially peroxisomal, and dually localized hetero-oligomers that access the peroxisome by piggyback import, localizing there in limited number, whereas the majority remain in the cytosol
IL is a homo-tetramer, chloramphenicol acetyltransferase (CAT) a homo-trimer and both carried a peroxisomal targeting signal type 1 (PTS1): IL is a natural protein of the plant peroxisome, and in the case of CAT, a PTS1 was added at the C-terminus
Summary
Peroxisomes are capable of importing folded and oligomeric proteins. it is a matter of dispute whether oligomer import by peroxisomes is the exception or the rule. I argue for a clear distinction between homo-oligomeric proteins that are essentially peroxisomal, and dually localized hetero-oligomers that access the peroxisome by piggyback import, localizing there in limited number, whereas the majority remain in the cytosol. There is evidence that binding by Pex5 in the cytosol can regulate their oligomerization state before import.
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