Molecular mechanism of perexisomal protein import into peroxisomes.

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To investigate the molecular mechanism of protein localization to peroxisome, we have found out several new facts as follows using in vitro import system of several peroxisomal proteins.1.Newly imported uricase in the in vitro import system quickly assembled to core structure found in the rat liver peroxisomes.2.We investigated the importance of proline residue near the C-terminal PTS-1 signal, which is frequently obserbed in the flanking regions of the protein-protein interaction sites.3.ATP hydrolysis is essential for acyl-CoA oxidase and uricase import into peroxisomes, and other three nucleotide tri-phosphates, such as GTP,CTP or UTP can substitute for ATP4.The molecular chaperone such as mitochondrial import stimulation factor (MSF) and HSC70, which are important for the mitochondrial protein translocation to mitochondria, has no essential role for the peroxisomal protein import into peroxisomes. We showed the presence of unidentified proteineous factor (S) essential for peroxisomal import.5.We developed the in vitro translocation of serine : pyruvate aminotransferase (SPT) into peroxisomes, and found that the association of peroxisomal SPT with the peroxisomal membrane cause a marked confomational change in the structure of this protein.