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

• Published in: Biochimica et biophysica acta Vol. 1216; no. 1; pp. 119 - 122
• Main Authors: Turley, Shannon J., Tan, Eng M., Pollard, K.Michael
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 19.10.1993; Elsevier
• Subjects: Amino Acid Sequence; Animals; Base Sequence; Biological and medical sciences; cDNA sequence; Chromosomal Proteins, Non-Histone - biosynthesis; Chromosomal Proteins, Non-Histone - genetics; Cloning, Molecular; Fibrillarin; Fundamental and applied biological sciences. Psychology; GAR domain; Genes. Genome; Interspecies amino acid sequence homology; Mice; Molecular and cellular biology; Molecular genetics; Molecular Sequence Data; Open Reading Frames; RNA, Small Nuclear - chemistry; RNA-binding motif; cDNA sequence; Interspecies amino acid sequence homology; Fibrillarin; GAR domain; RNA-binding motif; Vertebrata; Mammalia; Complementary DNA; Mouse; Nucleotide sequence; RNA binding protein; Rodentia; Sequence alignment; Homology; Nucleolus; Nuclear protein; Aminoacid sequence
• ISSN: 0167-4781; 0006-3002; 1879-2634
• DOI: 10.1016/0167-4781(93)90046-G

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.