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• W2103261658 abstract "In this study of the type 2 peroxisomal targeting signal (PTS2) pathway, we examined the apparent discontinuity and conservation of residues within the PTS2 nonapeptide and demonstrated that this topogenic signal is capable of directing heteromultimeric protein import in plant cells. Based on cumulative data showing that at least 26 unique, putative PTS2 nonapeptides occur within 12 diverse peroxisomal-destined proteins, the current (-R/K-L/V/I-X5-H/Q-L/A-) as well as the original (-R-L-X5-H/Q-L-) PTS2 motif appear to be oversimplified. To assess the functionality of residues within the motif, rat liver thiolase (rthio) and various chimeric chloramphenicol acetyltransferase (CAT) proteins were expressed transiently in suspension-cultured tobacco ( Nicotiana tabacum L.) cv Bright Yellow cells (BY-2), and their subcellular location was determined by immunofluorescence microscopy. Hemagglutinin (HA)-epitope-tagged-CAT subunits, lacking a PTS2 (CAT-HA), were ‘piggybacked’ into glyoxysomes by PTS2-bearing CAT subunits (rthio-CAT), whereas signal-depleted CAT-HA subunits that were modified to prevent oligomerization did not import into glyoxysomes. These results provided direct evidence that signal-depleted subunits imported into peroxisomes were targeted to the organelle as oligomers (heteromers) by a PTS2. Mutational analysis of residues within PTS2 nonapeptides revealed that a number of amino acid substitutions were capable of maintaining targeting function. Furthermore, functionality of residues within the PTS2 nonapeptide did not appear to require a context-specific environment conferred by adjacent residues. These results collectively suggest that the functional PTS2 is not solely defined as a sequence-specific motif, i.e. -R/K-X6-H/Q-A/L/F-, but defined also by its structural motif that is dependent upon the physiochemical properties of residues within the nonapeptide." @default.
• W2103261658 created "2016-06-24" @default.
• W2103261658 creator A5017296081 @default.
• W2103261658 creator A5017712570 @default.
• W2103261658 creator A5056780778 @default.
• W2103261658 date "1998-12-01" @default.
• W2103261658 modified "2023-10-17" @default.
• W2103261658 title "Mutational analyses of a type 2 peroxisomal targeting signal that is capable of directing oligomeric protein import into tobacco BY-2 glyoxysomes" @default.
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• W2103261658 doi "https://doi.org/10.1046/j.1365-313x.1998.00344.x" @default.
• W2103261658 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/10069077" @default.
• W2103261658 hasPublicationYear "1998" @default.
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