Molecular Cloning of Xenopus Fibrillarin, a Conserved U3 Small Nuclear Ribonucleoprotein Recognized by Antisera from Humans with Autoimmune Disease
| Autor: | B, Lapeyre, P, Mariottini, C, Mathieu, P, Ferrer, F, Amaldi, F, Amalric, M, Caizergues-Ferrer |
|---|---|
| Rok vydání: | 1990 |
| Předmět: |
Binding Sites
Base Sequence Chromosomal Proteins Non-Histone Molecular Sequence Data Cell Biology Blotting Northern Ribonucleoproteins Small Nuclear Autoantigens Recombinant Proteins Autoimmune Diseases Xenopus laevis Ribonucleoproteins RNA Small Nuclear Animals Amino Acid Sequence Cloning Molecular Molecular Biology Research Article |
| Zdroj: | Molecular and Cellular Biology. 10:430-434 |
| ISSN: | 1098-5549 |
| DOI: | 10.1128/mcb.10.1.430-434.1990 |
| Popis: | Autoantibodies against U3 small nuclear ribonucleoprotein are associated with scleroderma autoimmune disease. They were shown to react with fibrillarin, a 34- to 36-kilodalton protein that has been detected in all eukaryotes tested from humans to yeasts. We isolated a 1.6-kilobase cDNA encoding fibrillarin from a Xenopus laevis cDNA library. The protein contains a 79-residue-long Gly-Arg-rich domain in its N-terminal region and a putative RNA-binding domain with ribonucleoprotein consensus sequence in its central portion. This is the first report of cloning of fibrillarin, and the deduced protein sequence is in agreement with the involvement of the protein in a ribonucleoprotein particle. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|