Grünler J, Parmryd I
Department of Biochemistry, Stockholm University, Sweden.
FEBS Lett. 1999 Jul 23;455(3):233-7. doi: 10.1016/s0014-5793(99)00892-3.
Farnesyl protein transferase (FPT) activity was measured in rat liver subcellular fractions by using an unspecific acceptor for the farnesyl groups. The highest specific activity was found in mitochondria and it exceeded that of the microsomes three-fold. Considerably lower specific activities were found in the nuclei and cytosol. Further subfractionation revealed that the mitochondrial FPT activity is located in the matrix. The beta-subunit of the mitochondrial enzyme has an apparent molecular mass of 46 kDa, which is similar to its cytosolic counterpart. The results suggest that protein farnesylation can take place in a number of subcellular organelles.
利用法尼基基团的非特异性受体,测定了大鼠肝脏亚细胞组分中法尼基蛋白转移酶(FPT)的活性。在线粒体中发现了最高的比活性,其比微粒体中的比活性高出三倍。在细胞核和细胞质中发现的比活性则低得多。进一步的亚分级分离表明,线粒体FPT活性位于基质中。线粒体酶的β亚基的表观分子量为46 kDa,与其胞质对应物相似。结果表明,蛋白质法尼基化可在多种亚细胞器中发生。