Abstract: This chapter outlines the import of protein into peroxisomes. The first section reveals the discovery and metabolic functions of peroxisomes and highlights that peroxisomes were the last of the major subcellular organelles to be discovered. Unlike the nucleus, mitochondrion and chloroplast, peroxisomes have no DNA. Therefore, all of their polypeptide components are encoded by nuclear genes, synthesized on cytoplasmic polyribosomes, and then, transported post-translationally to peroxisomes. Peroxisomal membrane proteins (PMPs) embedded in the organelle membrane use membrane PTSs (mPTSs) for their targeting. These have been characterized in several proteins but have little in common except for a basic region. Early experiments on the peroxisomal targeting of reporter and endogenous proteins in the late 1980s showed that similar PTSs were used from yeast to humans. The alternative model is one in which the PTS receptors recognize cargo in the cytosol and shuttle them to the peroxisome. For the few PMPs whose targeting has been analyzed in vitro, the process is independent of ATE but dependent on cytosolic factors. For the few PMPs whose targeting has been analyzed in vitro, the process is independent of ATE but dependent on cytosolic factors. This chapter also highlights peroxisome inheritance and biogenesis intermediates along with a brief note on disorders involving peroxisomes.
Publication Year: 2002
Publication Date: 2002-01-01
Language: en
Type: book-chapter
Indexed In: ['crossref']
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Cited By Count: 3
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