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A more recent version of this article appeared on October 1, 2002
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Submitted on March 8, 2002
Revised on June 18, 2002
Accepted on July 22, 2002
1 Department of Molecular Biology and Functional Genomics, Stockholm University, SE-106 91, Stockholm, Sweden
2 Department of Biosciences at Novum, and Center for Genomics and Bioinformatics, Karolinska Institutet, Alfred Nobels Alle 10, Södertörns Högskola, Box 4101, SE-141 04 Huddinge, Sweden
3 Ludwig Institute for Cancer Research, Box 595, SE-751 24 Uppsala, Sweden
* Corresponding author. E-mail address: Lars.Wieslander{at}molbio.su.se.
Synthesis of the ribosomal subunits from pre-rRNA requires a large number of trans-acting proteins and snoRNPs to execute base modifications, RNA cleavages and structural rearrangements. We have characterized a novel protein, RBD-1 (RNA-Binding Domain-1), that is involved in ribosome biogenesis. This protein contains six consensus RNA-binding domains and is conserved as to sequence, domain organization and cellular location from yeast to human. RBD-1 is essential in Caenorhabditis elegans. In the dipteran Chironomus tentans, RBD-1 (Ct-RBD-1), binds pre-rRNA in vitro and anti-Ct-RBD-1 antibodies repress pre-rRNA processing in vivo. Ct-RBD-1 is mainly located in the nucleolus in an RNA polymerase I transcription dependent manner, but is also present in discrete foci in the interchromatin and in the cytoplasm. In cytoplasmic extracts, 20-30% of Ct-RBD-1 is associated with ribosomes and, preferentially with the 40S ribosomal subunit. Our data suggest that RBD-1 plays a role in structurally coordinating pre-rRNA during ribosome biogenesis and that this function is conserved in all eukaryotes.
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