Molecular cloning of Xenopus fibrillarin, a conserved U3 small nuclear ribonucleoprotein recognized by antisera from humans with autoimmune disease.

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.
AuthorsB Lapeyre, P Mariottini, C Mathieu, P Ferrer, F Amaldi, F Amalric, M Caizergues-Ferrer
JournalMolecular and cellular biology (Mol Cell Biol) Vol. 10 Issue 1 Pg. 430-4 (Jan 1990) ISSN: 0270-7306 [Print] UNITED STATES
PMID2136767 (Publication Type: Journal Article)
Chemical References
  • Autoantigens
  • Chromosomal Proteins, Non-Histone
  • RNA, Small Nuclear
  • Recombinant Proteins
  • Ribonucleoproteins
  • Ribonucleoproteins, Small Nuclear
  • fibrillarin
  • Amino Acid Sequence
  • Animals
  • Autoantigens (immunology)
  • Autoimmune Diseases (immunology)
  • Base Sequence
  • Binding Sites
  • Blotting, Northern
  • Chromosomal Proteins, Non-Histone (genetics)
  • Cloning, Molecular
  • Molecular Sequence Data
  • RNA, Small Nuclear (metabolism)
  • Recombinant Proteins
  • Ribonucleoproteins (genetics)
  • Ribonucleoproteins, Small Nuclear
  • Xenopus laevis (genetics)

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