Document Detail


Two splice variants of Nopp140 in Drosophila melanogaster.
MedLine Citation:
PMID:  11809845     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The Nopp140 gene of Drosophila maps within 79A5 of chromosome 3. Alternative splicing yields two variants. DmNopp140 (654 residues) is the sequence homolog 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 dense fibrillar components. In HeLa cells, DmNopp140-RGG localizes to intact nucleoli, whereas DmNopp140 partitions HeLa nucleoli into phase-light and phase-dark regions. The phase-light regions contain DmNopp140 and endogenous fibrillarin, whereas the phase-dark regions contain endogenous nucleolin. When coexpressed, both Drosophila variants colocalize to HeLa cell nucleoli. Both variants fail to localize to endogenous Cajal bodies 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 Cajal bodies, 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.
Authors:
John M Waggener; Patrick J DiMario
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, U.S. Gov't, Non-P.H.S.    
Journal Detail:
Title:  Molecular biology of the cell     Volume:  13     ISSN:  1059-1524     ISO Abbreviation:  Mol. Biol. Cell     Publication Date:  2002 Jan 
Date Detail:
Created Date:  2002-01-25     Completed Date:  2002-05-06     Revised Date:  2013-04-17    
Medline Journal Info:
Nlm Unique ID:  9201390     Medline TA:  Mol Biol Cell     Country:  United States    
Other Details:
Languages:  eng     Pagination:  362-81     Citation Subset:  IM    
Affiliation:
Department of Biological Sciences, Louisiana State University, Baton Rouge, LA 70803-1715, USA.
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MeSH Terms
Descriptor/Qualifier:
Alternative Splicing*
Amino Acid Motifs
Amino Acid Sequence
Animals
Cell Nucleolus / metabolism
Cells, Cultured
Chromosome Mapping
Drosophila Proteins / chemistry,  genetics*,  metabolism
Drosophila melanogaster / genetics,  metabolism*
Female
Fluorescent Antibody Technique
HeLa Cells
Humans
Molecular Sequence Data
Nuclear Proteins / chemistry,  genetics*,  metabolism
Oocytes / metabolism
Phosphoproteins / chemistry,  genetics*,  metabolism
Phosphorylation
Protein Structure, Tertiary
RNA, Messenger / metabolism
RNA-Binding Proteins / chemistry,  genetics,  metabolism
Sequence Homology, Amino Acid
Transfection
Xenopus
Chemical
Reg. No./Substance:
0/Drosophila Proteins; 0/NOLC1 protein, human; 0/Nolc1 protein, rat; 0/Nopp140 protein, Drosophila; 0/Nuclear Proteins; 0/Phosphoproteins; 0/RNA, Messenger; 0/RNA-Binding Proteins
Comments/Corrections

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