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

Lapeyre, Bruno; Mariottini, Paolo; Mathieu, C.; Ferrer, P.; Amaldi, Francesco; Amalríc, François; Caizergues‐Ferrer, Michèle

doi:10.1128/mcb.10.1.430

Cited by 115 publications

(66 citation statements)

References 28 publications

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“…Recently, the complementary DNA genes for fibrillarin from yeasts, frogs, and humans have been isolated and sequenced, revealing a high degree of homology in their primary structure during evolution (16)(17)(18)(19). AntL(U3)snRNP in SSc patients' sera can react with antigen derived from these 3 species (18,19).…”

Section: Discussionmentioning

confidence: 99%

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Autoantibody to U3 Nucleolar Ribonucleoprotein (Fibrillarin) In Patients with Systemic Sclerosis

Okano

Steen

Medsger

1992

Arthritis & Rheumatism

175

105

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To determine the clinical significance of serum antibodies to the U3 small nuclear ribonucleoprotein particle ([U3]snRNP), we studied sera from 416 patients with systemic sclerosis (SSc) and 264 controls, using immunofluorescence and immunoprecipitation assays. The presence of serum antb(U3)snRNP was highly specific to SSc, was found more frequently in blacks, and was associated with skeletal muscle disease and primary pulmonary arterial hypertension. These antibodies may identify one or more unusual clinical subsets of ssc.

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Section: Discussionmentioning

confidence: 99%

“…AntL(U3)snRNP in SSc patients' sera can react with antigen derived from these 3 species (18,19). (U3)snRNP is likely to be implicated in ribosomal RNA processing (5,20).…”

Section: Discussionmentioning

confidence: 99%

Autoantibody to U3 Nucleolar Ribonucleoprotein (Fibrillarin) In Patients with Systemic Sclerosis

Okano

Steen

Medsger

1992

Arthritis & Rheumatism

175

105

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“…Preparation of Recombinant and in Vitro Translated Proteins-Fulllength cDNA clones encoding Xenopus fibrillarin (37) and SMN (obtained in our two-hybrid screens) as well as human U1A (generously provided by Walther van Venrooij, University of Nijmegen) were subcloned into the glutathione S-transferase (GST) fusion expression vector, pZEX, in which the multiple cloning site of pGEX-2T (Amersham Pharmacia Biotech) was modified to shift the reading frame. 2 Proteins were expressed in Escherichia coli strain BL21 (room temperature induction, 5 h, 1 mM isopropyl-1-thio-␤-D-galactopyranoside) and purified using glutathione-agarose (Pierce).…”

Section: Methodsmentioning

confidence: 99%

Direct Interaction of the Spinal Muscular Atrophy Disease Protein SMN with the Small Nucleolar RNA-associated Protein Fibrillarin

Jones¹,

Gorzynski²,

Hales³

et al. 2001

Journal of Biological Chemistry

151

133

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Fibrillarin is one of four proteins known to interact selectively with all Box C/D family small nucleolar (sno) 1 RNAs (1-6). In eukaryotes, large numbers of snoRNAs direct cleavages and specific nucleotide modifications of pre-rRNA that are required for ribosome biogenesis (7-11). Most Box C/D family snoRNAs guide the site-specific 2Ј-O-methylation of rRNA (12,13). snoRNAs function as RNA-protein complexes known as small nucleolar ribonucleoprotein particles (snoRNPs) (11,14).Fibrillarin has sequence and structural homology to known methyltransferases (15, 16). This observation, coupled with functional studies in yeast (17), has led to the hypothesis that fibrillarin is the catalytic factor in Box C/D snoRNA-directed 2Ј-O-methylation of ribosomal RNA.The survival motor neuron (SMN) protein is linked with one of the most common inheritable causes of childhood mortality, spinal muscular atrophy (SMA) (18 -21). The SMN1 gene is deleted or mutated in patients with SMA (22) resulting in loss of spinal motor neurons accompanied by progressive muscular atrophy.SMN has been implicated in an array of cellular pathways. Antibody inhibition experiments have demonstrated that SMN is required for the biogenesis of spliceosomal small nuclear RNPs (snRNPs) (23, 24), and studies using in vitro splicing systems and yeast mutants have demonstrated a key role for SMN in pre-mRNA splicing (25-27). SMN has also been implicated in regulation of gene expression at the transcriptional level (28,29), in the assembly of the polymerase II transcription machinery (30), and as a neuron-specific anti-apoptotic factor (31-33).To learn more about snoRNP biogenesis and structure, we performed a yeast two-hybrid screen for proteins that interact with Xenopus fibrillarin. We identified the survival motor neuron (SMN) gene multiple times in screens of both Xenopus and human cDNA libraries. Fibrillarin had been detected previously in a two-hybrid screen using SMN (34). We have now demonstrated an in vivo interaction between SMN and fibrillarin, and we show that the two proteins interact directly in vitro. We have mapped the domains of each protein responsible for the interaction, and we found that SMN interacts with fibrillarin and the SmB snRNP protein via the same domain. Our findings suggest a function for SMN in the biogenesis and/or function of snoRNPs (similar to its established role with snRNPs (23-26, 35, 36)).EXPERIMENTAL PROCEDURES

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“…FIB, or Nop1p in the yeast Saccharomyces cerevisiae, is highly conserved in eukaryotes with respect to sequence, structure, and function (11)(12)(13)(14)(15)(16)(17). Deletion of the Nop1 gene in yeast results in inhibition of 2Ј-O-ribose methylation and pre-rRNA processing at sites A 0 to A 2 , indicating that Nop1p is directly involved in both pre-rRNA methylation and processing and ultimately in ribosome assembly (18).…”

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confidence: 99%

Human Fibrillarin Forms a Sub-complex with Splicing Factor 2-associated p32, Protein Arginine Methyltransferases, and Tubulins α3 and β1 That Is Independent of Its Association with Preribosomal Ribonucleoprotein Complexes

Yanagida

Hayano

Yamauchi

et al. 2004

Journal of Biological Chemistry

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Fibrillarin (FIB, Nop1p in yeast) is an RNA methyltransferase found not only in the fibrillar region of the nucleolus but also in Cajal bodies. FIB is essential for efficient processing of preribosomal RNA during ribosome biogenesis, although its precise function in this process and its role in Cajal bodies remain uncertain. Here, we demonstrate that the human FIB N-terminal glycine-and arginine-rich domain (residues 1-77) and its spacer region 1 (78 -132) interact with splicing factor 2-associated p32 (SF2A-p32) and that the FIB methyltransferase-like domain (133-321) interacts with protein-arginine methyltransferase 5 (PRMT5, Janus kinase-binding protein 1). We also show that these proteins associate with several additional proteins, including PRMT1, tubulin ␣3, and tubulin ␤1 to form a sub-complex that is principally independent of the association of FIB with preribosomal ribonucleoprotein complexes that co-immunoprecipitate with the sub-complex in human cells expressing FLAG-tagged FIB. Based on the physical association of FIB with SF2A-p32 and PRMTs, as well as the other reported results, we propose that FIB may coordinate both RNA and protein methylation during the processes of ribosome biogenesis in the nucleolus and RNA editing such as small nuclear (nucleolar) ribonucleoprotein biogenesis in Cajal bodies.Fibrillarin (FIB) 1 is the most abundant protein in the fibrillar regions of the nucleolus where ribosomal RNA transcription and early preribosomal RNA (pre-rRNA) processing take place (1, 2). FIB is also found in Cajal bodies, subnuclear organelles that contain distinct components involved in RNA transcription and editing such as mRNA splicing and small nuclear (nucleolar) ribonucleoprotein (sn(o)RNP) biogenesis (3, 4). FIB is a component of a ribonucleoprotein (RNP) complex that contains U3, U8, and U13 small nucleolar RNAs that exhibit consensus sequence elements denoted box C (5Ј-UGAUGA-3Ј) and box D (5Ј-CUGA-3Ј) (5). The FIB RNP associates with Nop56p, Nop5p/58p, and a 15.5-kDa protein (a counterpart of yeast Snu13p) to form box C/D snoRNP complexes that function in site-specific 2Ј-O-methylation of pre-rRNA (6 -9). FIB is the methyltransferase that catalyzes this 2Ј-O-methylation (10).FIB, or Nop1p in the yeast Saccharomyces cerevisiae, is highly conserved in eukaryotes with respect to sequence, structure, and function (11-17). Deletion of the Nop1 gene in yeast results in inhibition of 2Ј-O-ribose methylation and pre-rRNA processing at sites A 0 to A 2 , indicating that Nop1p is directly involved in both pre-rRNA methylation and processing and ultimately in ribosome assembly (18). Although human FIB is the functional homolog of yeast Nop1p, it only partially complements a yeast nop1-defective mutant (15). Human FIB is a nucleolar autoantigen for the non-hereditary immune disease scleroderma (14). FIB co-localizes with the survival motor neuron (SMN) gene product in both nucleoli and Cajal bodies/gems of primary neurons (19,20). SMN is linked to one of the most common inheritable causes of childho...

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

Cited by 115 publications

References 28 publications

Autoantibody to U3 Nucleolar Ribonucleoprotein (Fibrillarin) In Patients with Systemic Sclerosis

Autoantibody to U3 Nucleolar Ribonucleoprotein (Fibrillarin) In Patients with Systemic Sclerosis

Direct Interaction of the Spinal Muscular Atrophy Disease Protein SMN with the Small Nucleolar RNA-associated Protein Fibrillarin

Human Fibrillarin Forms a Sub-complex with Splicing Factor 2-associated p32, Protein Arginine Methyltransferases, and Tubulins α3 and β1 That Is Independent of Its Association with Preribosomal Ribonucleoprotein Complexes

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