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Publication : Molecular cloning and sequence analysis of U3 snoRNA-associated mouse fibrillarin.

First Author  Turley SJ Year  1993
Journal  Biochim Biophys Acta Volume  1216
Issue  1 Pages  119-22
PubMed ID  8218401 Mgi Jnum  J:15452
Mgi Id  MGI:63573 Doi  10.1016/0167-4781(93)90046-g
Citation  Turley SJ, et al. (1993) Molecular cloning and sequence analysis of U3 snoRNA-associated mouse fibrillarin. Biochim Biophys Acta 1216(1):119-22
abstractText  We have isolated and determined the sequence of a 1.1-kb cDNA from a murine WEHI-3 macrophage library which encodes the highly conserved, nucleolar protein, fibrillarin. The murine fibrillarin protein sequence displays 94.2% identity with human fibrillarin, 82.9% identity with amphibian fibrillarin and 74.0% identity with the yeast fibrillarin homolog, NOP1. Immunoprecipitation showed that anti-fibrillarin autoantibodies from human scleroderma sera and the monoclonal autoantibody 72B9 recognize the approx. 34-36 kDa in vitro transcribed and translated protein. Mouse fibrillarin contains a N-terminal glycine- and arginine-rich (GAR) domain which although conserved among the fibrillarins is not as strongly conserved as several regions in the carboxy tail of the protein. Specific amino acid residues in yeast NOP1 thought to be associated with the synthesis and maturation of ribosomes show strong conservation between the mouse, human, amphibian and yeast protein sequences.
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