Fibrillarin is a highly conserved component of a nucleolar small ribonucleoprotein complex in mammals, involved in the processing of ribosomal RNA during ribosomal biogenesis. The protein runs at ~35kDa on SDS-PAGE and is very rich in basic amino acids having a PI of 9.8. Fibrillarin was originally identified in humans since autoantibodies staining nucleoli were seen in some patients with the autoimmune disease scleroderma. Subsequently the protein fibrillarin was found to be the human homologue of Nop1p, a Saccharomyces cerevisiae nucleolar protein, the two proteins being 67% identical. We have generated an alignment of the sequences of fibrillarin and homologues downloadable from here. The fibrillarin molecule consists of an N-terminal glycine and arginine rich region followed by a highly conserved globular domain. Embryonic knockout of the fibrillarin gene in mice is lethal, suggesting fundamental importance of this protein. Autoantibodies to fibrillarin are also seen in patients with the autoimmune disease systemic sclerocis.
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