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Title: Mitochondrial and peroxisomal targeting of 2-methylacyl-CoA racemase in humans
Authors: Amery, Leen
Fransen, Marc
De Nys, Katelijne
Mannaerts, Guy
Van Veldhoven, Paul P # ×
Issue Date: Nov-2000
Series Title: Journal of lipid research. vol:41 issue:11 pages:1752-1759
Abstract: 2-Methylacyl-CoA racemase is an auxiliary enzyme required for the peroxisomal beta-oxidative breakdown of (2R)-pristanic acid and the (25R)-isomer of C(27) bile acid intermediates. The enzyme activity is found not only in peroxisomes but also is present in mitochondria of human liver and fibroblasts. The C terminus of the human racemase, a protein of 382 amino acids with a molecular mass of 43,304 daltons as deduced from its cloned cDNA, consists of KASL. Hitherto this sequence has not been recognized as a peroxisomal targeting signal (PTS1). From the in vitro interaction between recombinant racemase and recombinant human PTS1 receptor (Pex5p), and the peroxisomal localization of green fluorescent protein (GFP) fused to the N terminus of full-length racemase or its last six amino acids in tranfected Chinese hamster ovary (CHO) cells, we concluded that ASL is a new PTS1 variant. To be recognized by Pex5p, however, the preceding lysine residue is critical. As shown in another series of transfection experiments with GFP fused to the C terminus of the full-length racemase or racemase with deletions of the N terminus, mitochondrial targeting information is localized between amino acids 22 and 85.Hence, our data show that a single transcript gives rise to a racemase protein containing two topogenic signals, explaining the dual cellular localization of the activity.
URI: 
ISSN: 0022-2275
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Pharmacology Section (-)
Laboratory of Lipid Biochemistry and Protein Interactions
Department of Pharmaceutical & Pharmacological Sciences - miscellaneous
× corresponding author
# (joint) last author

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