Tollervey D
European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.
Mol Biol Rep. 1995;22(2-3):75-9. doi: 10.1007/BF00988709.
RNase MRP cleaves the yeast pre-rRNA at a site in internal transcribed spacer 1 (ITS1) and this cleavage can be reproduced in vitro by the highly purified enzyme. Two protein components (Pop1p and Pop2p) have been identified which are common to yeast RNase MRP and RNase P. Moreover, purified RNase P can also cleave the pre-rRNA substrate in vitro, underlining the similarities between these particles. Genetic evidence suggests that RNase MRP functionally interacts with the snoRNPs which are required for other pre-RNA processing reactions.
核糖核酸酶MRP在内部转录间隔区1(ITS1)的一个位点切割酵母前体rRNA,并且这种切割可以在体外由高度纯化的该酶重现。已经鉴定出两种蛋白质成分(Pop1p和Pop2p),它们是酵母核糖核酸酶MRP和核糖核酸酶P所共有的。此外,纯化的核糖核酸酶P在体外也能切割前体rRNA底物,这突出了这些颗粒之间的相似性。遗传学证据表明,核糖核酸酶MRP在功能上与其他前体RNA加工反应所需的小核仁核糖核蛋白颗粒相互作用。