S. Miura et al., POSTTRANSLATIONAL IMPORT OF 3-KETOACYL-COA THIOLASE INTO RAT-LIVER PEROXISOMES IN-VITRO, Journal of Biochemistry, 115(6), 1994, pp. 1064-1068
Cell-free translation products of hepatic free polysomal RNA from a cl
ofibrate-treated rat were incubated at 26 degrees C for 0-60 min with
a post-heavy mitochondrial supernatant fraction from normal rat liver.
Exogenously added proteinase K-resistant precursor and mature forms o
f peroxisomal 3-ketoacyl-CoA thiolase were recovered in a particulate
fraction and increased with time. Both forms of thiolase cosedimented
with peroxisomes, when the proteinase K-treated import reaction mixtur
e was centrifuged in a sucrose density gradient. The in vitro import a
nd processing of thiolase precursors, types A and B, was likewise repr
oduced with highly purified peroxisomes. These results strongly sugges
t that the precursor form of 3-ketoacyl-CoA thiolase is translocated i
nto peroxisomes, apparently without tight coupling with proteolytic pr
ocessing to the mature protein.