| Literature DB >> 17081119 |
Andrey Damianov1, Michael Kann, William S Lane, Albrecht Bindereif.
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.Entities:
Mesh:
Substances:
Year: 2006 PMID: 17081119 DOI: 10.1515/BC.2006.182
Source DB: PubMed Journal: Biol Chem ISSN: 1431-6730 Impact factor: 3.915