Translocation of acyl-CoA oxidase into peroxisomes requires ATP hydrolysis but not a membrane potential.
Translocation of acyl-CoA oxidase into peroxisomes requires ATP hydrolysis but not a membrane potential.
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将酰基-COA氧化酶转移到过氧化物酶体中需要ATP水解，但不需要膜电位。
DOI：
10.1083/jcb.105.6.2915
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发表时间：
1987-12
影响因子：
7.8
通讯作者：
Lazarow, P B
中科院分区：
文献类型：
--
作者：
Imanaka, T;Small, G M;Lazarow, P B
在体外重组了一种新合成的蛋白质导入高纯度大鼠肝脏过氧化物体的系统。35S标记的酰基辅酶A氧化酶(AOX)以一种抗蛋白酶K的方式被掺入到过氧化体中。这种导入是特异的(不发生在线粒体上)，并且依赖于温度、时间和过氧化物体浓度。在最佳条件下，约有30%的[35S]AOX对蛋白酶产生抗性。AOX进入过氧化体可分为两个步骤：(A)在没有ATP的情况下，0℃时发生结合；(B)仅在26℃时发生易位，需要ATP的水解。GTP不能替代三磷酸腺苷，间氯苯肼、呋喃霉素或其他离子载体不能抑制转位。
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.