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MBC in Press, published online ahead of print December 7, 2001
Mol. Biol. Cell 10.1091/mbc.01-04-0162

A more recent version of this article appeared on January 1, 2002
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Submitted on April 4, 2001
Revised on August 31, 2001
Accepted on October 26, 2001

Two splice variants of Nopp140 in Drosophila melanogaster

John M. Waggener1 and Patrick J. DiMario1*

1 Department of Biological Sciences, Louisiana State University Baton Rouge, Louisiana

* Corresponding author. E-mail address: pdimari{at}unix1.sncc.lsu.edu.

The Nopp140 gene of Drosophila maps within 79A5 of chromosome 3. Alternative splicing yields two variants. DmNopp140 (654 residues) is the sequence homologue of vertebrate Nopp140. Its carboxy terminus is 64% identical to that of the prototypical rat Nopp140. DmNopp140-RGG (688 residues) is identical to DmNopp140 throughout its first 551 residues, but its carboxy terminus contains a glycine/arginine rich domain that is often found in RNA-binding proteins such as vertebrate nucleolin. Both Drosophila variants localize to nucleoli in Drosophila Schneider II cells and Xenopus oocytes, specifically within the DFCs. In HeLa cells, DmNopp140-RGG localizes to intact nucleoli, while DmNopp140 partitions HeLa nucleoli into phase-light and phase-dark regions. The phase-light regions contain DmNopp140 and endogenous fibrillarin while the phase-dark regions contain endogenous nucleolin. When co-expressed, both Drosophila variants co-localize to HeLa cell nucleoli. Both variants fail to localize to endogenous Cajal bodies (CBs) in Xenopus oocyte nuclei and in HeLa cell nuclei. Endogenous HeLa coilin, however, accumulates around the periphery of phase-light regions in cells expressing DmNopp140. The carboxy truncation (DmNopp140deltaRGG) also fails to localize to CBs, but it forms similar phase-light regions that peripherally accumulate endogenous coilin. Conversely, we see no unusual accumulation of coilin in cells expressing DmNopp140-RGG.




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