Peroxisomal and mitochondrial targeting of serine:pyruvate/alanine:glyoxylate aminotransferase in rat liver

Cell Biochemistry and Biophysics
T OdaS Miura

Abstract

Serine:pyruvate/alanine:glyoxylate aminotransferase (SPT or SPT/AGT) of rat liver is a unique enzyme of dual subcellular localization, and exists in both mitochondria and peroxisomes. To characterize a peroxisomal targeting signal of rat liver SPT, a number of C-terminal mutants were constructed and their subcellular localization in transfected COS-1 cells was examined. Deletion of C-terminal NKL, and point mutation of K2 (the second Lys from the C-terminus), K4 and E15 caused accumulation of translated products in the cytoplasm. This suggests that the PTS of SPT is not identical to PTS1 (the C-terminal SKL motif) in that it is not restricted to the C-terminal tripeptide. In vitro synthesized precursor for mitochondrial SPT was highly sensitive to the proteinase K digestion, whereas peroxisomal SPT (SPTp) was fairly resistant to the protease. In in vitro import experiment with purified peroxisomes, however, SPTp recovered in the peroxisomal fraction was very sensitive to the protease. These results suggest that the mitochondrial precursor is synthesized as an unfolded form and is translocated into the mitochondrial matrix, whereas SPTp is synthesized as a folded form and its conformation changes to an unfolded form just before ...Continue Reading

Citations

Dec 21, 2006·Histochemistry and Cell Biology·Werner J KovacsSkaidrite K Krisans
Nov 22, 2001·Proceedings of the National Academy of Sciences of the United States of America·C LaloiY Meyer
Nov 28, 2008·The Plant Journal : for Cell and Molecular Biology·Chris CarrieJames Whelan
Jan 21, 2006·The Journal of Nutrition·Tracy StitesRobert B Rucker
Feb 3, 2015·Journal of Cellular and Molecular Medicine·Isabel ValençaDaniela Ribeiro

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