Human RBM28 protein is a specific nucleolar component of the spliceosomal snRNPs

被引:17
作者
Damianov, Andrey
Kann, Michael
Lane, William S.
Bindereif, Albrecht
机构
[1] Univ Giessen, Inst Biochem, D-35392 Giessen, Germany
[2] Univ Giessen, Inst Med Virol, D-35392 Giessen, Germany
[3] Harvard Univ, Dept Mol & Cellular Biol, Harvard Microchem & Proteom Anal Facil, Cambridge, MA 02138 USA
关键词
nucleolus; snRNA; snRNP; splicing;
D O I
10.1515/BC.2006.182
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:1455 / 1460
页数:6
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