酰基辅酶A氧化酶转位至过氧化物酶体需要ATP水解，但不需要膜电位。
Translocation of acyl-CoA oxidase into peroxisomes requires ATP hydrolysis but not a membrane potential.
作者信息
Imanaka T, Small G M, Lazarow P B
机构信息
Rockefeller University, New York 10021.
出版信息
J Cell Biol. 1987 Dec;105(6 Pt 2):2915-22. doi: 10.1083/jcb.105.6.2915.
Abstract
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.
摘要
体外重建了一个高效的系统，用于将新合成的蛋白质导入高度纯化的大鼠肝脏过氧化物酶体。35S标记的酰基辅酶A氧化酶（AOx）以蛋白酶K抗性的方式整合到过氧化物酶体中。这种导入具有特异性（在线粒体中不发生），并且依赖于温度、时间和过氧化物酶体浓度。在最佳条件下，约30%的[35S]AOx变得对蛋白酶具有抗性。AOx导入过氧化物酶体可分为两个步骤：（a）在0℃且无ATP的情况下发生结合；（b）转位仅在26℃发生，且需要ATP水解。GTP不能替代ATP，羰基氰化物间氯苯腙、缬氨霉素或其他离子载体不会抑制转位。
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