Horng J T, Behari R, Burke L E, Baker A
Department of Biochemistry, University of Cambridge, England.
Eur J Biochem. 1995 May 15;230(1):157-63. doi: 10.1111/j.1432-1033.1995.tb20546.x.
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.
利用体外导入系统对乙醇酸氧化酶向过氧化物酶体的摄取进行了研究。发现乙醇酸氧化酶的导入依赖于ATP且依赖于温度，并且对乙醛酸循环体具有特异性。在这些方面，它类似于异柠檬酸裂解酶向乙醛酸循环体和叶型过氧化物酶体的导入；因此，ATP依赖性和温度依赖性似乎是植物微体蛋白导入的普遍特性。制备了乙醇酸氧化酶的两个突变体版本，分别缺失N端的59个氨基酸和C端的53个氨基酸。两者都能够进行依赖于ATP的导入，而由与乙醇酸氧化酶的最后20个氨基酸相连的胞质蛋白二氢叶酸还原酶组成的融合蛋白与乙醛酸循环体结合，但没有进入细胞器。
