title: Investigation of the energy requirement and targeting signal for the import of glycolate oxidase into glyoxysomes.
abstract: The uptake of glycolate oxidase into peroxisomes has been studied using an in vitro import system. Import of glycolate oxidase was found to be ATP-dependent and temperature-dependent and specific for glyoxysomes. In these respects it resembles the import of isocitrate lyase into both glyoxysomes and leaf-type peroxisomes; thus the ATP-dependence and temperature dependence appear to be general properties of plant microbody protein import. Two mutant versions of glycolate oxidase were prepared lacking 59 amino acids of the N-terminus and 53 amino acids of C-terminus, respectively. Both were capable of ATP-dependent import, whereas a fusion protein consisting of the cytosolic protein dihydrofolate reductase linked to the last 20 amino acids of glycolate oxidase bound to glyoxysomes but did not enter the organelle.
authors.affiliation: Department of Biochemistry, University of Cambridge, England.
authors.forename: J T
authors.initials: JT
authors.lastname: Horng
authors.forename: R
authors.initials: R
authors.lastname: Behari
authors.forename: L E
authors.initials: LE
authors.lastname: Burke
authors.forename: A
authors.initials: A
authors.lastname: Baker
mesh_terms: D000255:Adenosine Triphosphate / Q000502:physiology; D000429:Alcohol Oxidoreductases / Q000737:chemistry / Q000378:metabolism*; D000595:Amino Acid Sequence; D001483:Base Sequence; D008830:Microbodies / Q000201:enzymology*; D008969:Molecular Sequence Data; D017510:Protein Folding; D013762:Tetrahydrofolate Dehydrogenase / Q000378:metabolism
chemical_list: D000255:Adenosine Triphosphate; D000429:Alcohol Oxidoreductases; C020821:glycollate oxidase; D013762:Tetrahydrofolate Dehydrogenase