Damianov Andrey, Kann Michael, Lane William S, Bindereif Albrecht
Institut für Biochemie, Justus-Liebig-Universität Giessen, Heinrich-Buff-Ring 58, D-35392 Giessen, Germany.
Biol Chem. 2006 Oct-Nov;387(10-11):1455-60. doi: 10.1515/BC.2006.182.
The biogenesis of spliceosomal small nuclear RNAs (snRNAs) involves organized translocations between the cytoplasm and certain nuclear domains, such as Cajal bodies and nucleoli. Here we identify human RBM28 protein as a novel snRNP component, based on affinity selection of U6 small nuclear ribonucleoprotein (snRNP). As shown by immunofluorescence, RBM28 is a nucleolar protein. Anti-RBM28 immunoprecipitation from HeLa cell lysates revealed that this protein specifically associates with U1, U2, U4, U5, and U6 snRNAs. Our data provide the first evidence that RBM28 is a common nucleolar component of the spliceosomal ribonucleoprotein complexes, possibly coordinating their transition through the nucleolus.
剪接体小核RNA(snRNA)的生物合成涉及细胞质与某些核结构域(如 Cajal 体和核仁)之间的有序转运。在此,我们基于U6小核核糖核蛋白(snRNP)的亲和选择,鉴定出人类RBM28蛋白是一种新型的snRNP组分。免疫荧光显示,RBM28是一种核仁蛋白。从HeLa细胞裂解物中进行的抗RBM28免疫沉淀表明,该蛋白特异性地与U1、U2、U4、U5和U6 snRNA结合。我们的数据首次证明,RBM28是剪接体核糖核蛋白复合物的一种常见核仁组分,可能在协调它们通过核仁的转变过程中发挥作用。