Castaño J G, Ornberg R, Koster J G, Tobian J A, Zasloff M
Cell. 1986 Aug 1;46(3):377-85. doi: 10.1016/0092-8674(86)90658-6.
In eukaryotes pre-tRNA species are processed at the 5' end by an endonuclease. Here we describe the first characterization of the structure of a eukaryotic pre-tRNA 5' processing endonuclease. The 5' pre-tRNAase, isolated from X. laevis ovaries, copurifies with a 16S macromolecular complex consisting of at least 14 polypeptides ranging in MW from about 20,000 to 32,000. These polypeptides comprise a cylindrical particle, apparently organized as a stack of four rings, similar or identical to a ubiquitous eukaryotic subcellular particle described in the literature over the past 15 years. Similar copurification is observed for the enzyme from HeLa cells, suggesting that the X. laevis enzyme is representative of a general class of eukaryotic pre-tRNA 5' processing nuclease.
在真核生物中,前体tRNA物种在5'端由一种核酸内切酶进行加工。在此,我们描述了真核生物前体tRNA 5'加工核酸内切酶结构的首次表征。从非洲爪蟾卵巢中分离出的5'前体tRNA酶与一个16S大分子复合物共同纯化,该复合物由至少14种多肽组成,分子量范围约为20,000至32,000。这些多肽构成一个圆柱形颗粒,显然组织成四层堆叠的环,类似于或等同于过去15年文献中描述的一种普遍存在的真核亚细胞颗粒。从HeLa细胞中提取的该酶也观察到类似的共同纯化现象,这表明非洲爪蟾的这种酶代表了真核生物前体tRNA 5'加工核酸酶的一类普遍类型。