Journal article

Publication year: 2006

Pages: 1455-1460

Journal: Biological Chemistry

Volume number: 387

Issue number: 10-11

ISSN: 1431-6730

eISSN: 1437-4315

DOI Link: https://doi.org/10.1515/BC.2006.182

Publisher: De Gruyter Brill

Abstract: 
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.

Harvard Citation style: Damianov, A., Kann, M., Lane, W. and Bindereif, A. (2006) Human RBM28 protein is a specific nucleolar component of the spliceosomal snRNPs, Biological Chemistry, 387(10-11), pp. 1455-1460. https://doi.org/10.1515/BC.2006.182

APA Citation style: Damianov, A., Kann, M., Lane, W., & Bindereif, A. (2006). Human RBM28 protein is a specific nucleolar component of the spliceosomal snRNPs. Biological Chemistry. 387(10-11), 1455-1460. https://doi.org/10.1515/BC.2006.182