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NOP58 Nop58p

Nop58p, Nop58, Nop5
component of the box C/D class of small nucleolar ribonucleoprotein particles (snoRNPs); may catalyze the modification of ribosomal RNAs [RGD, Feb 2006] (from NCBI)
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Top mentioned proteins: Nop56, CAN, 15.5K, POLYMERASE, NOP17
Papers on Nop58p
Structure/Function Analysis of Protein-Protein Interactions Developed by the Yeast Pih1 Platform Protein and Its Partners in Box C/D snoRNP Assembly.
Manival et al., Vandœuvre-lès-Nancy, France. In J Mol Biol, Sep 2015
By co-expression in Escherichia coli, we demonstrate that Pih1p has two other direct partners, the Rsa1p assembly factor and the Nop58p core protein, and in vivo and in vitro experiments mapped the required binding domains.
Nop17 is a key R2TP factor for the assembly and maturation of box C/D snoRNP complex.
Oliveira et al., São Paulo, Brazil. In Bmc Mol Biol, 2014
BACKGROUND: Box C/D snoRNPs are responsible for rRNA methylation and processing, and are formed by snoRNAs and four conserved proteins, Nop1, Nop56, Nop58 and Snu13.
Fibrillarin methylates H2A in RNA polymerase I trans-active promoters in Brassica oleracea.
Castano et al., Mérida, Mexico. In Front Plant Sci, 2014
In plants, fibrillarin binds directly the guide RNA together with Nop56, Nop58, and 15.5ka proteins to form a snoRNP complex that selects the sites to be methylated in pre-processing of ribosomal RNA.
Proteomic and 3D structure analyses highlight the C/D box snoRNP assembly mechanism and its control.
Bertrand et al., Montpellier, France. In J Cell Biol, 2014
This revealed several unexpected features: (a) the existence of a protein-only pre-snoRNP complex containing five assembly factors and two core proteins, 15.5K and Nop58; (b) the characterization of ZNHIT3, which is present in the protein-only complex but gets released upon binding to C/D snoRNAs; (c) the dynamics of the R2TP complex, which appears to load/unload RuvBL AAA(+) adenosine triphosphatase from pre-snoRNPs; and (d) a potential mechanism for preventing premature activation of snoRNP catalytic activity.
Identification of discrete classes of small nucleolar RNA featuring different ends and RNA binding protein dependency.
Scott et al., Sherbrooke, Canada. In Nucleic Acids Res, 2014
Surprisingly, the long forms are more dependent than the short forms on the expression of the core snoRNP protein NOP58, thought to be essential for C/D snoRNA production.
Oligogenic germline mutations identified in early non-smokers lung adenocarcinoma patients.
Frullanti et al., Siena, Italy. In Lung Cancer, 2014
Some of these mutant genes (such as BAG6, SPEN and WISP3) are recognized as major cancer players in lung tumors; others have been previously identified in other human cancers (JAK2, TCEB3C, NELFE, TAF1B, EBLN2), in mouse models (GON4L, NOP58, and RBMX) or in genome-wide association studies (KIAA2018, ZNF311).
RNA-Seq of the nucleolus reveals abundant SNORD44-derived small RNAs.
Laiho et al., Baltimore, United States. In Plos One, 2013
The expression of the SNORD44 sdRNA and 120 nt form was independent of Dicer/Drosha-mediated processing pathways but was dependent on the box C/D snoRNP proteins/sno-ribonucleoproteins fibrillarin and NOP58.
Nutritional status modulates box C/D snoRNP biogenesis by regulated subcellular relocalization of the R2TP complex.
Houry et al., In Genome Biol, 2013
BACKGROUND: Box C/D snoRNPs, which are typically composed of box C/D snoRNA and the four core protein components Nop1, Nop56, Nop58, and Snu13, play an essential role in the modification and processing of pre-ribosomal RNA.
Alu-mediated nonallelic homologous and nonhomologous recombination in the BMPR2 gene in heritable pulmonary arterial hypertension.
Gamou et al., Tokyo, Japan. In Genet Med, 2013
For cases in which exons 1-3 were deleted, the 5' and 3' break points were located in the AluY repeat sequences in the 5' side of the adjacent NOP58 gene and in the AluY repeat sequences in intron 3, suggesting an AluY-mediated nonallelic homologous recombination as the mechanism responsible for the deletion.
Protein Hit1, a novel box C/D snoRNP assembly factor, controls cellular concentration of the scaffolding protein Rsa1 by direct interaction.
Charpentier et al., Vandœuvre-lès-Nancy, France. In Nucleic Acids Res, 2013
Nop58p/NOP58, Nop56p/NOP56 and Nop1p/Fibrillarin on box C/D small nucleolar RNAs (C/D snoRNAs).
CRM1 plays a nuclear role in transporting snoRNPs to nucleoli in higher eukaryotes.
Bertrand et al., Montpellier, France. In Nucleus, 2012
We show that Tgs1 LF is exported by CRM1 and that interaction with CRM1 competes for binding with the C-terminal domain of the core protein Nop58, which contains the Nucleolar localization signal of Box C/D snoRNPs (NoLS).
Composition of yeast snRNPs and snoRNPs in the absence of trimethylguanosine caps reveals nuclear cap binding protein as a gained U1 component implicated in the cold-sensitivity of tgs1Δ cells.
Shuman et al., New York City, United States. In Nucleic Acids Res, 2011
Moreover, CBP was not associated with mature Nop58-containing C/D snoRNPs or mature Cbf5- and Gar1-containing H/ACA snoRNPs from tgs1Δ cells.
A role for SUMOylation in snoRNP biogenesis revealed by quantitative proteomics.
Lamond et al., Dundee, United Kingdom. In Nucleus, 2011
A role for SUMOylation in the biogenesis and/or function of Box C/D snoRNPs has been reported, mediated via SUMO2 conjugation to the core snoRNP protein, Nop58.
A proteomic screen for nucleolar SUMO targets shows SUMOylation modulates the function of Nop5/Nop58.
Lamond et al., Dundee, United Kingdom. In Mol Cell, 2010
SUMOylation is essential for high-affinity Nop58 binding to small nucleolar riboproteins.
Evidence that the AAA+ proteins TIP48 and TIP49 bridge interactions between 15.5K and the related NOP56 and NOP58 proteins during box C/D snoRNP biogenesis.
Watkins et al., Newcastle upon Tyne, United Kingdom. In Mol Cell Biol, 2009
snoRNP assembly factor NUFIP can regulate the interactions between TIP48 and TIP49 and the core box C/D proteins.
Binding of the human Prp31 Nop domain to a composite RNA-protein platform in U4 snRNP.
Wahl et al., Göttingen, Germany. In Science, 2007
Although highly homologous, the spliceosomal hPrp31 and the nucleolar Nop56 and Nop58 (Nop56/58) proteins recognize different ribonucleoprotein (RNP) particles.
Biogenesis and intranuclear trafficking of human box C/D and H/ACA RNPs.
Weber et al., Toulouse, France. In Cold Spring Harb Symp Quant Biol, 2005
The box C/D snoRNAs associate with fibrillarin, Nop56, Nop58, and 15.5K/NHPX proteins to form functional snoRNP particles, whereas all box H/ACA snoRNAs form complexes with the dyskerin, Nop10, Nhp2, and Gar1 snoRNP proteins.
Characterization of Saccharomyces cerevisiae Nop17p, a novel Nop58p-interacting protein that is involved in Pre-rRNA processing.
Oliveira et al., São Paulo, Brazil. In J Mol Biol, 2005
Nop17p depletion leads to mislocalization of Nop1p, Nop56p, Nop58p and Snu13p, which are the core proteins of the box C/D ribonucleoprotein
Mammalian and yeast U3 snoRNPs are matured in specific and related nuclear compartments.
Bertrand et al., Montpellier, France. In Embo J, 2002
Mammalian and yeast U3 snoRNPs are matured in specific and related nuclear compartments.
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