|SMART accession number:||SM01206|
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- Evolution (species in which this domain is found)
Taxonomic distribution of proteins containing Fibrillarin domain.
This tree includes only several representative species. The complete taxonomic breakdown of all proteins with Fibrillarin domain is also avaliable.
Click on the protein counts, or double click on taxonomic names to display all proteins containing Fibrillarin domain in the selected taxonomic class.
- Literature (relevant references for this domain)
Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Pellizzoni L, Baccon J, Charroux B, Dreyfuss G
- The survival of motor neurons (SMN) protein interacts with the snoRNP proteinsfibrillarin and GAR1.
- Curr Biol. 2001; 11: 1079-88
- Display abstract
BACKGROUND: The survival of motor neurons (SMN) protein is the protein product ofthe spinal muscular atrophy (SMA) disease gene. SMN and its associated proteinsGemin2, Gemin3, and Gemin4 form a large complex that plays a role in snRNPassembly, pre-mRNA splicing, and transcription. The functions of SMN in theseprocesses are mediated by a direct interaction of SMN with components of thesemachineries, such as Sm proteins and RNA helicase A. RESULTS: We show that SMNbinds directly to fibrillarin and GAR1. Fibrillarin and GAR1 are specific markersof the two classes of small nucleolar ribonucleoprotein particles (snoRNPs) that are involved in posttranscriptional processing and modification of ribosomal RNA.SMN interaction requires the arginine- and glycine-rich domains of bothfibrillarin and GAR1 and is defective in SMN mutants found in some SMA patients. Coimmunoprecipitations demonstrate that the SMN complex associates withfibrillarin and with GAR1 in vivo. The inhibition of RNA polymerase Itranscription causes a transient redistribution of SMN to the nucleolar peripheryand loss of fibrillarin and GAR1 colocalization with SMN in gems. Furthermore,the expression of a dominant-negative mutant of SMN (SMNDeltaN27) causes snoRNPs to accumulate outside of the nucleolus in structures that also contain componentsof gems and coiled (Cajal) bodies. CONCLUSIONS: These findings identifyfibrillarin and GAR1 as novel interactors of SMN and suggest a function for theSMN complex in the assembly and metabolism of snoRNPs. We propose that the SMNcomplex performs functions necessary for the biogenesis and function of diverseribonucleoprotein complexes.
- Structure (3D structures containing this domain)
3D Structures of Fibrillarin domains in PDB
PDB code Main view Title 1fbn CRYSTAL STRUCTURE OF A FIBRILLARIN HOMOLOGUE FROM METHANOCOCCUS JANNASCHII, A HYPERTHERMOPHILE, AT 1.6 A 1g8a PYROCOCCUS HORIKOSHII FIBRILLARIN PRE-RRNA PROCESSING PROTEIN 1g8s METHANOCOCCUS JANNASCHII FIBRILLARIN PRE-RRNA PROCESSING PROTEIN 1nt2 CRYSTAL STRUCTURE OF FIBRILLARIN/NOP5P COMPLEX 1pry Structure Determination of Fibrillarin Homologue From Hyperthermophilic Archaeon Pyrococcus furiosus (Pfu-65527) 2ipx Human Fibrillarin 2nnw Alternative conformations of Nop56/58-fibrillarin complex and implication for induced-fit assenly of box C/D RNPs 3id5 Crystal structure of Sulfolobus solfataricus C/D RNP assembled with Nop5, fibrillarin, L7Ae and a split half C/D RNA 3id6 Crystal structure of Sulfolobus solfataricus Nop5 (1-262) and fibrillarin complex 3nmu Crystal Structure of substrate-bound halfmer box C/D RNP 3nvk Structural basis for substrate placement by an archaeal box C/D ribonucleoprotein particle 3nvm Structural basis for substrate placement by an archaeal box C/D ribonucleoprotein particle 3pla Crystal structure of a catalytically active substrate-bound box C/D RNP from Sulfolobus solfataricus 4by9 The structure of the Box CD enzyme reveals regulation of rRNA methylation 4df3 Crystal Structure of Aeropyrum pernix fibrillarin in complex with natively bound S-adenosyl-L-methionine at 1.7A
- Links (links to other resources describing this domain)