Andrey Damianov, 1. Institut für Biochemie, Justus-Liebig-Universität Giessen, Heinrich-Buff-Ring 58, D-35392 Giessen, Germany and Present address: Howard Hughes Medical Institute, University of California Los Angeles, Los Angeles, CA 90095-1662, USA
1 Michael Kann, 2. Institut für Medizinische Virologie, Justus-Liebig-Universität Giessen, Frankfurter Str. 107, D-35392 Giessen, Germany and Present address: UMR 5097 REGER, CNRS-Université Victor Segalen Bordeaux 2, 146 rue Léo Saignat, F-33076 Bordeaux cedex, France
2 William S. Lane, 3. Harvard Microchemistry and Proteomics Analysis Facility, Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138, USA
3 Albrecht Bindereif4. Institut für Biochemie, Justus-Liebig-Universität Giessen, Heinrich-Buff-Ring 58, D-35392 Giessen, Germany
4 Corresponding author
Citation Information. Biological Chemistry. Volume 387, Issue 10/11, Pages 1455–1460, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: 10.1515/BC.2006.182, October/November
Publication History: Received: //; accepted: //; published online: 02/11/2006
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.
Keywords nucleolus, snRNA, snRNP, splicing
