Artigo Acesso aberto Revisado por pares

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

1990; Taylor & Francis; Volume: 10; Issue: 1 Linguagem: Inglês

10.1128/mcb.10.1.430

ISSN

1098-5549

Autores

Bruno Lapeyre, Paolo Mariottini, Chantal Mathieu, Pierre Ferrer, Francesco Amaldi, F. Amalric, M. Caizergues-Ferrer,

Tópico(s)

RNA and protein synthesis mechanisms

Resumo

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.

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