Translocation of acyl-CoA oxidase into peroxisomes requires ATP hydrolysis but not a membrane potential.
An efficient system for the import of newly synthesized proteins into highly purified rat liver peroxisomes was reconstituted in vitro. 35S-Labeled acyl-CoA oxidase (AOx) was incorporated into peroxisomes in a proteinase K-resistant fashion. This import was specific (did not occur with mitochondria) and was dependent on temperature, time, and peroxisome concentration. Under optimal conditions approximately 30% of [35S]AOx became proteinase resistant. The import of AOx into peroxisomes could be dissociated into two steps: (a) binding occurred at 0 degrees C in the absence of ATP; (b) translocation occurred only at 26 degrees C and required the hydrolysis of ATP. GTP would not substitute for ATP and translocation was not inhibited by carbonylcyanide-m-chlorophenylhydrazone, valinomycin, or other ionophores.
Rockefeller University, New York 10021.
T
T
Imanaka
G M
GM
Small
P B
PB
Lazarow
D042962:Acyl-CoA Oxidase; D000255:Adenosine Triphosphate / Q000378:metabolism; D001693:Biological Transport, Active; D002258:Carbonyl Cyanide m-Chlorophenyl Hydrazone / Q000494:pharmacology; D002458:Cell Fractionation; D002499:Centrifugation, Density Gradient; D066298:In Vitro Techniques; D007472:Iohexol; D007476:Ionophores / Q000494:pharmacology; D007700:Kinetics; D008274:Magnesium / Q000494:pharmacology; D015636:Magnesium Chloride; D008564:Membrane Potentials; D008830:Microbodies / Q000378:metabolism*; D010088:Oxidoreductases / Q000378:metabolism*; D011189:Potassium Chloride / Q000494:pharmacology; D013696:Temperature
D007476:Ionophores; D015636:Magnesium Chloride; D007472:Iohexol; D002258:Carbonyl Cyanide m-Chlorophenyl Hydrazone; D011189:Potassium Chloride; D000255:Adenosine Triphosphate; D010088:Oxidoreductases; D042962:Acyl-CoA Oxidase; D008274:Magnesium