Fibrillarin: Difference between revisions

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{{Orphan|date=July 2007}}
{{Infobox_gene}}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox protein family
{{PBB_Controls
| Symbol = Fibrillarin
| update_page = yes
| Name = Fibrillarin
| require_manual_inspection = no
| image = PDB 1g8a EBI.jpg
| update_protein_box = yes
| width = 250
| update_summary = yes
| caption = pyrococcus horikoshii fibrillarin pre-rrna processing protein
| update_citations = yes
| Pfam = PF01269
| Pfam_clan = CL0063
| InterPro = IPR000692
| SMART =
| PROSITE = PDOC00489
| MEROPS =
| SCOP = 1fbn
| TCDB =  
| OPM family =  
| OPM protein =  
| CAZy =  
| CDD =  
}}
}}
'''rRNA 2'-O-methyltransferase fibrillarin''' is an [[enzyme]] that in humans is encoded by the ''FBL'' [[gene]].<ref name="pmid1846968">{{cite journal | vauthors = Aris JP, Blobel G | title = cDNA cloning and sequencing of human fibrillarin, a conserved nucleolar protein recognized by autoimmune antisera | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 88 | issue = 3 | pages = 931–5 | date = Feb 1991 | pmid = 1846968 | pmc = 50928 | doi = 10.1073/pnas.88.3.931 }}</ref><ref name="pmid2026646">{{cite journal | vauthors = Jansen RP, Hurt EC, Kern H, Lehtonen H, Carmo-Fonseca M, Lapeyre B, Tollervey D | title = Evolutionary conservation of the human nucleolar protein fibrillarin and its functional expression in yeast | journal = The Journal of Cell Biology | volume = 113 | issue = 4 | pages = 715–29 | date = May 1991 | pmid = 2026646 | pmc = 2288999 | doi = 10.1083/jcb.113.4.715 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: FBL fibrillarin| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2091| accessdate = }}</ref>


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image = PBB_Protein_FBL_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2ipx.
| PDB = {{PDB2|2ipx}}
| Name = Fibrillarin
| HGNCid = 3599
| Symbol = FBL
| AltSymbols =; FIB; FLRN; RNU3IP1
| OMIM = 134795
| ECnumber = 
| Homologene = 1099
| MGIid = 95486
| GeneAtlas_image1 = PBB_GE_FBL_211623_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003723 |text = RNA binding}} {{GNF_GO|id=GO:0008168 |text = methyltransferase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0030529 |text = ribonucleoprotein complex}}
| Process = {{GNF_GO|id=GO:0006364 |text = rRNA processing}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 2091
    | Hs_Ensembl = ENSG00000105202
    | Hs_RefseqProtein = NP_001427
    | Hs_RefseqmRNA = NM_001436
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 19
    | Hs_GenLoc_start = 45016938
    | Hs_GenLoc_end = 45028848
    | Hs_Uniprot = P22087
    | Mm_EntrezGene = 14113
    | Mm_Ensembl = 
    | Mm_RefseqmRNA = NM_007991
    | Mm_RefseqProtein = NP_032017
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 
    | Mm_GenLoc_start = 
    | Mm_GenLoc_end = 
    | Mm_Uniprot = 
  }}
}}
'''Fibrillarin''', also known as '''FBL''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: FBL fibrillarin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2091| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
This gene product is a component of a nucleolar small nuclear ribonucleoprotein (snRNP) particle thought to participate in the first step in processing pre-ribosomal (r)RNA. It is associated with the [[Small nucleolar RNA U3|U3]], [[U8 small nucleolar RNA|U8]], and [[U13 small nucleolar RNA|U13]] small nucleolar RNAs and is located in the dense fibrillar component (DFC) of the [[nucleolus]]. The encoded protein contains an N-terminal repetitive domain that is rich in glycine and arginine residues, like fibrillarins in other species. Its central region resembles an RNA-binding domain and contains an RNP consensus sequence. Antisera from approximately 8% of humans with the autoimmune disease [[scleroderma]] recognize fibrillarin.<ref name="entrez"/>
{{PBB_Summary
| section_title =
| summary_text = This gene product is a component of a nucleolar small nuclear ribonucleoprotein (snRNP) particle thought to participate in the first step in processing preribosomal RNA. It is associated with the U3, U8, and U13 small nuclear RNAs and is located in the dense fibrillar component (DFC) of the nucleolus. The encoded protein contains an N-terminal repetitive domain that is rich in glycine and arginine residues, like fibrillarins in other species. Its central region resembles an RNA-binding domain and contains an RNP consensus sequence. Antisera from approximately 8% of humans with the autoimmune disease scleroderma recognize fibrillarin.<ref name="entrez">{{cite web | title = Entrez Gene: FBL fibrillarin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2091| accessdate = }}</ref>
}}


Fibrillarin is a component of several ribonucleoproteins including a nucleolar small nuclear ribonucleoprotein ([[SnRNP]]) and one of the two classes of [[snoRNA|small nucleolar ribonucleoproteins]] (snoRNPs). SnRNAs function in [[Splicing (genetics)|RNA splicing]] while snoRNPs function in [[Ribosomal RNA|ribosomal]] [[RNA]] processing.  
Fibrillarin is a component of several ribonucleoproteins including a nucleolar small nuclear ribonucleoprotein ([[SnRNP]]) and one of the two classes of [[snoRNA|small nucleolar ribonucleoproteins]] (snoRNPs). SnRNAs function in [[Splicing (genetics)|RNA splicing]] while snoRNPs function in [[ribosomal RNA]] processing.  


Fibrillarin is associated with U3, U8 and U13 [[small nuclear RNA]]s in mammals and is similar to the yeast NOP1 protein. Fibrillarin has a well conserved sequence of around 320 amino acids, and contains 3 domains, an N-terminal Gly/Arg-rich region; a central domain resembling other RNA-binding proteins and containing an RNP-2-like consensus sequence; and a C-terminal alpha-helical domain. An evolutionarily related pre-rRNA processing protein, which lacks the Gly/Arg-rich domain, has been found in various archaebacteria.
Fibrillarin is associated with U3, U8 and U13 [[small nuclear RNA]]s in mammals and is similar to the yeast NOP1 protein. Fibrillarin has a well conserved sequence of around 320 amino acids, and contains 3 domains, an N-terminal Gly/Arg-rich region; a central domain resembling other RNA-binding proteins and containing an RNP-2-like consensus sequence; and a C-terminal alpha-helical domain. An evolutionarily related pre-rRNA processing protein, which lacks the Gly/Arg-rich domain, has been found in various archaebacteria.


A study by Schultz et al indicated that the K-turn binding 15.5-kDa protein (called Snu13 in yeast) interacts with [[spliceosome]] proteins hPRP31, hPRP3, hPRP4, CYPH and the [[snoRNA|small nucleolar ribonucleoproteins]] NOP56, NOP58, and fibrillarin. The 15.5-kDa protein has sequence similarity to other RNA-binding proteins such as ribosomal proteins S12, L7a, and L30 and the [[snoRNA|snoRNP]] protein NHP2. The U4/U6 snRNP contains 15.5-kDa protein<ref>[http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pubmed&pubmedid=16782898 Protein-Protein and Protein-RNA Contacts both Contribute to the 15.5K-Mediated Assembly of the U4/U6 snRNP and the Box C/D snoRNPs] by Annemarie Schultz, Stephanie Nottrott, Nicholas James Watkins and Reinhard Lührmann in ''Molecular and Cellular Biology'' (2006) Volume 26, pages 5146–5154.</ref>. The 15.5-kDa protein also exists in a ribonucleoprotein complex that binds the U3 box B/C motif. The 15.5-kDa protein also exists as one of the four core proteins of the [[snoRNA|C/D small nucleolar ribonucleoprotein]] that mediates methylation of pre-ribosomal RNAs.
A study by Schultz et al. indicated that the K-turn binding 15.5-kDa protein (called Snu13 in yeast) interacts with [[spliceosome]] proteins hPRP31, hPRP3, hPRP4, CYPH and the small nucleolar ribonucleoproteins [[NOL5A|NOP56]], [[NOP5/NOP58|NOP58]], and fibrillarin. The 15.5-kDa protein has sequence similarity to other RNA-binding proteins such as ribosomal proteins S12, L7a, and L30 and the snoRNP protein [[NOLA2|NHP2]]. The U4/U6 snRNP contains 15.5-kDa protein.<ref>[http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pubmed&pubmedid=16782898 Protein-Protein and Protein-RNA Contacts both Contribute to the 15.5K-Mediated Assembly of the U4/U6 snRNP and the Box C/D snoRNPs] by Annemarie Schultz, Stephanie Nottrott, Nicholas James Watkins and Reinhard Lührmann in ''Molecular and Cellular Biology'' (2006) Volume 26, pages 5146–5154.</ref> The 15.5-kDa protein also exists in a ribonucleoprotein complex that binds the U3 box B/C motif. The 15.5-kDa protein also exists as one of the four core proteins of the [[snoRNA|C/D small nucleolar ribonucleoprotein]] that mediates methylation of pre-ribosomal RNAs.


Structural evidence supporting the idea that fibrillarin is the [[snoRNA|small nucleolar ribonucleoprotein]] [[methyltransferase]] has been reviewed<ref>[http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pubmed&pubmedid=17284456 The structure and function of small nucleolar ribonucleoproteins] by Steve L. Reichow, Tomoko Hamma, Adrian R. Ferré-D'Amaré and Gabriele Varani in ''[[Nucleic Acids Research]]'' (2007) Volume 35, pages 1452–1464.</ref>.
Structural evidence supporting the idea that fibrillarin is the snoRNA [[methyltransferase]] has been reviewed.<ref>[http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pubmed&pubmedid=17284456 The structure and function of small nucleolar ribonucleoproteins] by Steve L. Reichow, Tomoko Hamma, Adrian R. Ferré-D'Amaré and Gabriele Varani in ''[[Nucleic Acids Research]]'' (2007) Volume 35, pages 1452–1464.</ref>


==References==
== Interactions ==
{{reflist|2}}
 
==Further reading==
Fibrillarin has been shown to [[Protein-protein interaction|interact]] with [[DDX5]]<ref name=pmid10837141>{{cite journal | vauthors = Nicol SM, Causevic M, Prescott AR, Fuller-Pace FV | title = The nuclear DEAD box RNA helicase p68 interacts with the nucleolar protein fibrillarin and colocalizes specifically in nascent nucleoli during telophase | journal = Experimental Cell Research | volume = 257 | issue = 2 | pages = 272–80 | date = Jun 2000 | pmid = 10837141 | doi = 10.1006/excr.2000.4886 }}</ref> and [[SMN1]].<ref name=pmid11509230>{{cite journal | vauthors = Pellizzoni L, Baccon J, Charroux B, Dreyfuss G | title = The survival of motor neurons (SMN) protein interacts with the snoRNP proteins fibrillarin and GAR1 | journal = Current Biology | volume = 11 | issue = 14 | pages = 1079–88 | date = Jul 2001 | pmid = 11509230 | doi = 10.1016/S0960-9822(01)00316-5 }}</ref>
 
== References ==
{{reflist}}
 
[[File:38F3-ChkNFH-DAPI-Shsy5y.jpg|thumb|Human [[neuroblastoma]], ([[SH-SY5Y]]) cells stained with antibody to fibrillarin in green, antibody to [[neurofilament]] NF-H in red and DNA in dark blue, The fibrillarin antibody binds to spots in the nucleus corresponding to nucleoli. The nucleoli also contain DNA and so appear as pale blue dots. The neurofilament NF-H antibody binds to cytoplasmic [[Intermediate_filament|intermediate or 10nm filaments]]. Image, antibodies and staining by [[EnCor Biotechnology Inc.]]]]
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Baserga SJ, Yang XD, Steitz JA | title = An intact Box C sequence in the U3 snRNA is required for binding of fibrillarin, the protein common to the major family of nucleolar snRNPs | journal = The EMBO Journal | volume = 10 | issue = 9 | pages = 2645–51 | date = Sep 1991 | pmid = 1714385 | pmc = 452965 | doi =  }}
| citations =
* {{cite journal | vauthors = Okano Y, Steen VD, Medsger TA | title = Autoantibody to U3 nucleolar ribonucleoprotein (fibrillarin) in patients with systemic sclerosis | journal = Arthritis and Rheumatism | volume = 35 | issue = 1 | pages = 95–100 | date = Jan 1992 | pmid = 1731817 | doi = 10.1002/art.1780350114 }}
*{{cite journal | author=Baserga SJ, Yang XD, Steitz JA |title=An intact Box C sequence in the U3 snRNA is required for binding of fibrillarin, the protein common to the major family of nucleolar snRNPs. |journal=EMBO J. |volume=10 |issue= 9 |pages= 2645-51 |year= 1991 |pmid= 1714385 |doi=  }}
* {{cite journal | vauthors = Lischwe MA, Ochs RL, Reddy R, Cook RG, Yeoman LC, Tan EM, Reichlin M, Busch H | title = Purification and partial characterization of a nucleolar scleroderma antigen (Mr = 34,000; pI, 8.5) rich in NG,NG-dimethylarginine | journal = The Journal of Biological Chemistry | volume = 260 | issue = 26 | pages = 14304–10 | date = Nov 1985 | pmid = 2414294 | doi =  }}
*{{cite journal | author=Okano Y, Steen VD, Medsger TA |title=Autoantibody to U3 nucleolar ribonucleoprotein (fibrillarin) in patients with systemic sclerosis. |journal=Arthritis Rheum. |volume=35 |issue= 1 |pages= 95-100 |year= 1992 |pmid= 1731817 |doi= }}
* {{cite journal | vauthors = Méhes G, Pajor L | title = Nucleolin and fibrillarin expression in stimulated lymphocytes and differentiating HL-60 cells. A flow cytometric assay | journal = Cell Proliferation | volume = 28 | issue = 6 | pages = 329–36 | date = Jun 1995 | pmid = 7626687 | doi = 10.1111/j.1365-2184.1995.tb00074.x }}
*{{cite journal | author=Aris JP, Blobel G |title=cDNA cloning and sequencing of human fibrillarin, a conserved nucleolar protein recognized by autoimmune antisera. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 3 |pages= 931-5 |year= 1991 |pmid= 1846968 |doi=  }}
* {{cite journal | vauthors = Liu Q, Dreyfuss G | title = A novel nuclear structure containing the survival of motor neurons protein | journal = The EMBO Journal | volume = 15 | issue = 14 | pages = 3555–65 | date = Jul 1996 | pmid = 8670859 | pmc = 451956 | doi =  }}
*{{cite journal | author=Jansen RP, Hurt EC, Kern H, ''et al.'' |title=Evolutionary conservation of the human nucleolar protein fibrillarin and its functional expression in yeast. |journal=J. Cell Biol. |volume=113 |issue= 4 |pages= 715-29 |year= 1991 |pmid= 2026646 |doi= }}
* {{cite journal | vauthors = Magoulas C, Zatsepina OV, Jordan PW, Jordan EG, Fried M | title = The SURF-6 protein is a component of the nucleolar matrix and has a high binding capacity for nucleic acids in vitro | journal = European Journal of Cell Biology | volume = 75 | issue = 2 | pages = 174–83 | date = Feb 1998 | pmid = 9548374 | doi = 10.1016/s0171-9335(98)80059-9 }}
*{{cite journal | author=Lischwe MA, Ochs RL, Reddy R, ''et al.'' |title=Purification and partial characterization of a nucleolar scleroderma antigen (Mr = 34,000; pI, 8.5) rich in NG,NG-dimethylarginine. |journal=J. Biol. Chem. |volume=260 |issue= 26 |pages= 14304-10 |year= 1985 |pmid= 2414294 |doi=  }}
* {{cite journal | vauthors = Ai LS, Lin CH, Hsieh M, Li C | title = Arginine methylation of a glycine and arginine rich peptide derived from sequences of human FMRP and fibrillarin | journal = Proceedings of the National Science Council, Republic of China. Part B, Life Sciences | volume = 23 | issue = 4 | pages = 175–80 | date = Oct 1999 | pmid = 10518318 | doi =  }}
*{{cite journal | author=Méhes G, Pajor L |title=Nucleolin and fibrillarin expression in stimulated lymphocytes and differentiating HL-60 cells. A flow cytometric assay. |journal=Cell Prolif. |volume=28 |issue= 6 |pages= 329-36 |year= 1995 |pmid= 7626687 |doi= }}
* {{cite journal | vauthors = Pintard L, Kressler D, Lapeyre B | title = Spb1p is a yeast nucleolar protein associated with Nop1p and Nop58p that is able to bind S-adenosyl-L-methionine in vitro | journal = Molecular and Cellular Biology | volume = 20 | issue = 4 | pages = 1370–81 | date = Feb 2000 | pmid = 10648622 | pmc = 85287 | doi = 10.1128/MCB.20.4.1370-1381.2000 }}
*{{cite journal | author=Liu Q, Dreyfuss G |title=A novel nuclear structure containing the survival of motor neurons protein. |journal=EMBO J. |volume=15 |issue= 14 |pages= 3555-65 |year= 1996 |pmid= 8670859 |doi=  }}
* {{cite journal | vauthors = Nicol SM, Causevic M, Prescott AR, Fuller-Pace FV | title = The nuclear DEAD box RNA helicase p68 interacts with the nucleolar protein fibrillarin and colocalizes specifically in nascent nucleoli during telophase | journal = Experimental Cell Research | volume = 257 | issue = 2 | pages = 272–80 | date = Jun 2000 | pmid = 10837141 | doi = 10.1006/excr.2000.4886 }}
*{{cite journal | author=Magoulas C, Zatsepina OV, Jordan PW, ''et al.'' |title=The SURF-6 protein is a component of the nucleolar matrix and has a high binding capacity for nucleic acids in vitro. |journal=Eur. J. Cell Biol. |volume=75 |issue= 2 |pages= 174-83 |year= 1998 |pmid= 9548374 |doi= }}
* {{cite journal | vauthors = Pellizzoni L, Baccon J, Charroux B, Dreyfuss G | title = The survival of motor neurons (SMN) protein interacts with the snoRNP proteins fibrillarin and GAR1 | journal = Current Biology | volume = 11 | issue = 14 | pages = 1079–88 | date = Jul 2001 | pmid = 11509230 | doi = 10.1016/S0960-9822(01)00316-5 }}
*{{cite journal | author=Ai LS, Lin CH, Hsieh M, Li C |title=Arginine methylation of a glycine and arginine rich peptide derived from sequences of human FMRP and fibrillarin. |journal=Proc. Natl. Sci. Counc. Repub. China B |volume=23 |issue= 4 |pages= 175-80 |year= 1999 |pmid= 10518318 |doi= }}
* {{cite journal | vauthors = Zhou X, Tan FK, Xiong M, Milewicz DM, Feghali CA, Fritzler MJ, Reveille JD, Arnett FC | title = Systemic sclerosis (scleroderma): specific autoantigen genes are selectively overexpressed in scleroderma fibroblasts | journal = Journal of Immunology | volume = 167 | issue = 12 | pages = 7126–33 | date = Dec 2001 | pmid = 11739535 | doi = 10.4049/jimmunol.167.12.7126 }}
*{{cite journal | author=Pintard L, Kressler D, Lapeyre B |title=Spb1p is a yeast nucleolar protein associated with Nop1p and Nop58p that is able to bind S-adenosyl-L-methionine in vitro. |journal=Mol. Cell. Biol. |volume=20 |issue= 4 |pages= 1370-81 |year= 2000 |pmid= 10648622 |doi= }}
* {{cite journal | vauthors = Andersen JS, Lyon CE, Fox AH, Leung AK, Lam YW, Steen H, Mann M, Lamond AI | title = Directed proteomic analysis of the human nucleolus | journal = Current Biology | volume = 12 | issue = 1 | pages = 1–11 | date = Jan 2002 | pmid = 11790298 | doi = 10.1016/S0960-9822(01)00650-9 }}
*{{cite journal | author=Nicol SM, Causevic M, Prescott AR, Fuller-Pace FV |title=The nuclear DEAD box RNA helicase p68 interacts with the nucleolar protein fibrillarin and colocalizes specifically in nascent nucleoli during telophase. |journal=Exp. Cell Res. |volume=257 |issue= 2 |pages= 272-80 |year= 2000 |pmid= 10837141 |doi= 10.1006/excr.2000.4886 }}
* {{cite journal | vauthors = Cimato TR, Tang J, Xu Y, Guarnaccia C, Herschman HR, Pongor S, Aletta JM | title = Nerve growth factor-mediated increases in protein methylation occur predominantly at type I arginine methylation sites and involve protein arginine methyltransferase 1 | journal = Journal of Neuroscience Research | volume = 67 | issue = 4 | pages = 435–42 | date = Feb 2002 | pmid = 11835310 | doi = 10.1002/jnr.10123 }}
*{{cite journal | author=Pellizzoni L, Baccon J, Charroux B, Dreyfuss G |title=The survival of motor neurons (SMN) protein interacts with the snoRNP proteins fibrillarin and GAR1. |journal=Curr. Biol. |volume=11 |issue= 14 |pages= 1079-88 |year= 2001 |pmid= 11509230 |doi= }}
* {{cite journal | vauthors = Fujiyama S, Yanagida M, Hayano T, Miura Y, Isobe T, Fujimori F, Uchida T, Takahashi N | title = Isolation and proteomic characterization of human Parvulin-associating preribosomal ribonucleoprotein complexes | journal = The Journal of Biological Chemistry | volume = 277 | issue = 26 | pages = 23773–80 | date = Jun 2002 | pmid = 11960984 | doi = 10.1074/jbc.M201181200 }}
*{{cite journal | author=Zhou X, Tan FK, Xiong M, ''et al.'' |title=Systemic sclerosis (scleroderma): specific autoantigen genes are selectively overexpressed in scleroderma fibroblasts. |journal=J. Immunol. |volume=167 |issue= 12 |pages= 7126-33 |year= 2001 |pmid= 11739535 |doi= }}
* {{cite journal | vauthors = Whitehead SE, Jones KW, Zhang X, Cheng X, Terns RM, Terns MP | title = Determinants of the interaction of the spinal muscular atrophy disease protein SMN with the dimethylarginine-modified box H/ACA small nucleolar ribonucleoprotein GAR1 | journal = The Journal of Biological Chemistry | volume = 277 | issue = 50 | pages = 48087–93 | date = Dec 2002 | pmid = 12244096 | doi = 10.1074/jbc.M204551200 }}
*{{cite journal | author=Andersen JS, Lyon CE, Fox AH, ''et al.'' |title=Directed proteomic analysis of the human nucleolus. |journal=Curr. Biol. |volume=12 |issue= 1 |pages= 1-11 |year= 2002 |pmid= 11790298 |doi= }}
* {{cite journal | vauthors = Herrera-Esparza R, Kruse L, von Essen M, Campos L, Barbosa O, Bollain JJ, Badillo I, Avalos-Díaz E | title = U3 snoRNP associates with fibrillarin a component of the scleroderma clumpy nucleolar domain | journal = Archives of Dermatological Research | volume = 294 | issue = 7 | pages = 310–7 | date = Oct 2002 | pmid = 12373336 | doi = 10.1007/s00403-002-0338-7 }}
*{{cite journal | author=Cimato TR, Tang J, Xu Y, ''et al.'' |title=Nerve growth factor-mediated increases in protein methylation occur predominantly at type I arginine methylation sites and involve protein arginine methyltransferase 1. |journal=J. Neurosci. Res. |volume=67 |issue= 4 |pages= 435-42 |year= 2002 |pmid= 11835310 |doi= }}
* {{cite journal | vauthors = Chen M, Rockel T, Steinweger G, Hemmerich P, Risch J, von Mikecz A | title = Subcellular recruitment of fibrillarin to nucleoplasmic proteasomes: implications for processing of a nucleolar autoantigen | journal = Molecular Biology of the Cell | volume = 13 | issue = 10 | pages = 3576–87 | date = Oct 2002 | pmid = 12388758 | pmc = 129967 | doi = 10.1091/mbc.02-05-0083 }}
*{{cite journal | author=Fujiyama S, Yanagida M, Hayano T, ''et al.'' |title=Isolation and proteomic characterization of human Parvulin-associating preribosomal ribonucleoprotein complexes. |journal=J. Biol. Chem. |volume=277 |issue= 26 |pages= 23773-80 |year= 2002 |pmid= 11960984 |doi= 10.1074/jbc.M201181200 }}
* {{cite journal | vauthors = Watkins NJ, Dickmanns A, Lührmann R | title = Conserved stem II of the box C/D motif is essential for nucleolar localization and is required, along with the 15.5K protein, for the hierarchical assembly of the box C/D snoRNP | journal = Molecular and Cellular Biology | volume = 22 | issue = 23 | pages = 8342–52 | date = Dec 2002 | pmid = 12417735 | pmc = 134055 | doi = 10.1128/MCB.22.23.8342-8352.2002 }}
*{{cite journal | author=Whitehead SE, Jones KW, Zhang X, ''et al.'' |title=Determinants of the interaction of the spinal muscular atrophy disease protein SMN with the dimethylarginine-modified box H/ACA small nucleolar ribonucleoprotein GAR1. |journal=J. Biol. Chem. |volume=277 |issue= 50 |pages= 48087-93 |year= 2003 |pmid= 12244096 |doi= 10.1074/jbc.M204551200 }}
*{{cite journal | author=Herrera-Esparza R, Kruse L, von Essen M, ''et al.'' |title=U3 snoRNP associates with fibrillarin a component of the scleroderma clumpy nucleolar domain. |journal=Arch. Dermatol. Res. |volume=294 |issue= 7 |pages= 310-7 |year= 2003 |pmid= 12373336 |doi= 10.1007/s00403-002-0338-7 }}
*{{cite journal  | author=Chen M, Rockel T, Steinweger G, ''et al.'' |title=Subcellular recruitment of fibrillarin to nucleoplasmic proteasomes: implications for processing of a nucleolar autoantigen. |journal=Mol. Biol. Cell |volume=13 |issue= 10 |pages= 3576-87 |year= 2003 |pmid= 12388758 |doi= 10.1091/mbc.02-05-0083 }}
*{{cite journal  | author=Watkins NJ, Dickmanns A, Lührmann R |title=Conserved stem II of the box C/D motif is essential for nucleolar localization and is required, along with the 15.5K protein, for the hierarchical assembly of the box C/D snoRNP. |journal=Mol. Cell. Biol. |volume=22 |issue= 23 |pages= 8342-52 |year= 2003 |pmid= 12417735 |doi=  }}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=2091}}


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Revision as of 05:55, 31 August 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human
Fibrillarin
File:PDB 1g8a EBI.jpg
pyrococcus horikoshii fibrillarin pre-rrna processing protein
Identifiers
SymbolFibrillarin
PfamPF01269
Pfam clanCL0063
InterProIPR000692
PROSITEPDOC00489
SCOP1fbn
SUPERFAMILY1fbn

rRNA 2'-O-methyltransferase fibrillarin is an enzyme that in humans is encoded by the FBL gene.[1][2][3]

Function

This gene product is a component of a nucleolar small nuclear ribonucleoprotein (snRNP) particle thought to participate in the first step in processing pre-ribosomal (r)RNA. It is associated with the U3, U8, and U13 small nucleolar RNAs and is located in the dense fibrillar component (DFC) of the nucleolus. The encoded protein contains an N-terminal repetitive domain that is rich in glycine and arginine residues, like fibrillarins in other species. Its central region resembles an RNA-binding domain and contains an RNP consensus sequence. Antisera from approximately 8% of humans with the autoimmune disease scleroderma recognize fibrillarin.[3]

Fibrillarin is a component of several ribonucleoproteins including a nucleolar small nuclear ribonucleoprotein (SnRNP) and one of the two classes of small nucleolar ribonucleoproteins (snoRNPs). SnRNAs function in RNA splicing while snoRNPs function in ribosomal RNA processing.

Fibrillarin is associated with U3, U8 and U13 small nuclear RNAs in mammals and is similar to the yeast NOP1 protein. Fibrillarin has a well conserved sequence of around 320 amino acids, and contains 3 domains, an N-terminal Gly/Arg-rich region; a central domain resembling other RNA-binding proteins and containing an RNP-2-like consensus sequence; and a C-terminal alpha-helical domain. An evolutionarily related pre-rRNA processing protein, which lacks the Gly/Arg-rich domain, has been found in various archaebacteria.

A study by Schultz et al. indicated that the K-turn binding 15.5-kDa protein (called Snu13 in yeast) interacts with spliceosome proteins hPRP31, hPRP3, hPRP4, CYPH and the small nucleolar ribonucleoproteins NOP56, NOP58, and fibrillarin. The 15.5-kDa protein has sequence similarity to other RNA-binding proteins such as ribosomal proteins S12, L7a, and L30 and the snoRNP protein NHP2. The U4/U6 snRNP contains 15.5-kDa protein.[4] The 15.5-kDa protein also exists in a ribonucleoprotein complex that binds the U3 box B/C motif. The 15.5-kDa protein also exists as one of the four core proteins of the C/D small nucleolar ribonucleoprotein that mediates methylation of pre-ribosomal RNAs.

Structural evidence supporting the idea that fibrillarin is the snoRNA methyltransferase has been reviewed.[5]

Interactions

Fibrillarin has been shown to interact with DDX5[6] and SMN1.[7]

References

  1. ↑ Aris JP, Blobel G (Feb 1991). "cDNA cloning and sequencing of human fibrillarin, a conserved nucleolar protein recognized by autoimmune antisera". Proceedings of the National Academy of Sciences of the United States of America. 88 (3): 931–5. doi:10.1073/pnas.88.3.931. PMC 50928. PMID 1846968.
  2. ↑ Jansen RP, Hurt EC, Kern H, Lehtonen H, Carmo-Fonseca M, Lapeyre B, Tollervey D (May 1991). "Evolutionary conservation of the human nucleolar protein fibrillarin and its functional expression in yeast". The Journal of Cell Biology. 113 (4): 715–29. doi:10.1083/jcb.113.4.715. PMC 2288999. PMID 2026646.
  3. ↑ 3.0 3.1 "Entrez Gene: FBL fibrillarin".
  4. ↑ Protein-Protein and Protein-RNA Contacts both Contribute to the 15.5K-Mediated Assembly of the U4/U6 snRNP and the Box C/D snoRNPs by Annemarie Schultz, Stephanie Nottrott, Nicholas James Watkins and Reinhard Lührmann in Molecular and Cellular Biology (2006) Volume 26, pages 5146–5154.
  5. ↑ The structure and function of small nucleolar ribonucleoproteins by Steve L. Reichow, Tomoko Hamma, Adrian R. Ferré-D'Amaré and Gabriele Varani in Nucleic Acids Research (2007) Volume 35, pages 1452–1464.
  6. ↑ Nicol SM, Causevic M, Prescott AR, Fuller-Pace FV (Jun 2000). "The nuclear DEAD box RNA helicase p68 interacts with the nucleolar protein fibrillarin and colocalizes specifically in nascent nucleoli during telophase". Experimental Cell Research. 257 (2): 272–80. doi:10.1006/excr.2000.4886. PMID 10837141.
  7. ↑ Pellizzoni L, Baccon J, Charroux B, Dreyfuss G (Jul 2001). "The survival of motor neurons (SMN) protein interacts with the snoRNP proteins fibrillarin and GAR1". Current Biology. 11 (14): 1079–88. doi:10.1016/S0960-9822(01)00316-5. PMID 11509230.
File:38F3-ChkNFH-DAPI-Shsy5y.jpg
Human neuroblastoma, (SH-SY5Y) cells stained with antibody to fibrillarin in green, antibody to neurofilament NF-H in red and DNA in dark blue, The fibrillarin antibody binds to spots in the nucleus corresponding to nucleoli. The nucleoli also contain DNA and so appear as pale blue dots. The neurofilament NF-H antibody binds to cytoplasmic intermediate or 10nm filaments. Image, antibodies and staining by EnCor Biotechnology Inc.

Further reading

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