Characterization of the sequences encoding for Xenopus laevis box C/D snoRNP Nop56 protein

Renzi, Fabiana; Filippini, Daniela; Loreni, Fabrizio; Bozzoni, Irene; Caffarelli, Elisa

doi:10.1016/s0167-4781(02)00233-6

Cited by 4 publications

(4 citation statements)

References 13 publications

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“…NOP56 is part of a core protein complex, along with NOP58, fibrillarin (FBL) and a 15.5 kD RNA-binding protein, of the C/D box small nucleolar ribonucleoprotein (snoRNP), which is in charge of cleavage and modification of precursor ribosomal RNAs (pre-rRNAs) and assembly of the 60S ribosomal subunit [ 1 , 2 , 3 ] Specifically, this C/D box snoRNP introduces a direct 2′-O-ribose methylation in specific residues in pre-rRNA and is involved in the endonucleolytic cleavages of the 35S rRNA primary transcript [ 4 ]. This C/D complex is highly conserved throughout evolution from archaea to humans [ 3 , 5 , 6 , 7 , 8 , 9 ].…”

Section: Introductionmentioning

confidence: 99%

A nop56 Zebrafish Loss-of-Function Model Exhibits a Severe Neurodegenerative Phenotype

et al. 2022

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NOP56 belongs to a C/D box small nucleolar ribonucleoprotein complex that is in charge of cleavage and modification of precursor ribosomal RNAs and assembly of the 60S ribosomal subunit. An intronic expansion in NOP56 gene causes Spinocerebellar Ataxia type 36, a typical late-onset autosomal dominant ataxia. Although vertebrate animal models were created for the intronic expansion, none was studied for the loss of function of NOP56. We studied a zebrafish loss-of-function model of the nop56 gene which shows 70% homology with the human gene. We observed a severe neurodegenerative phenotype in nop56 mutants, characterized mainly by absence of cerebellum, reduced numbers of spinal cord neurons, high levels of apoptosis in the central nervous system (CNS) and impaired movement, resulting in death before 7 days post-fertilization. Gene expression of genes related to C/D box complex, balance and CNS development was impaired in nop56 mutants. In our study, we characterized the first NOP56 loss-of-function vertebrate model, which is important to further understand the role of NOP56 in CNS function and development.

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Section: Introductionmentioning

confidence: 99%

A nop56 Zebrafish Loss-of-Function Model Exhibits a Severe Neurodegenerative Phenotype

et al. 2022

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“…Nevertheless, some snoRNAs can also be processed by endonucleolytic cleavage in the intron sequences flanking the snoRNA (Fragapane et al, 1993). XendoU is the first endoribonuclease involved in the processing of snoRNAs in higher eukaryotes to be described and is involved in the processing of at least two snoRNAs in Xenopus laevis oocytes (Fragapane et al, 1993;Caffarelli et al, 1994;Renzi et al, 2002;Laneve et al, 2003). It is a U-specific enzyme that, uniquely among known endoribonucleases, releases 2 0 -3 0 cyclic phosphate termini using Mn 2+ as an essential cofactor.…”

Section: Introductionmentioning

confidence: 99%

Large-scale purification and crystallization of the endoribonuclease XendoU: troubleshooting with His-tagged proteins

et al. 2006

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XendoU is the first endoribonuclease described in higher eukaryotes as being involved in the endonucleolytic processing of intron-encoded small nucleolar RNAs. It is conserved among eukaryotes and its viral homologue is essential in SARS replication and transcription. The large-scale purification and crystallization of recombinant XendoU are reported. The tendency of the recombinant enzyme to aggregate could be reversed upon the addition of chelating agents (EDTA, imidazole): aggregation is a potential drawback when purifying and crystallizing His-tagged proteins, which are widely used, especially in high-throughput structural studies. Purified monodisperse XendoU crystallized in two different space groups: trigonal P3(1)21, diffracting to low resolution, and monoclinic C2, diffracting to higher resolution.

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“…All box C/D snoRNAs bind to the 2Ј-O-methyltransferase fibrillarin/Nop1 (18,78,86,88), as well as Nop56 (22,71), Nop58 (47,53), and 15.5-kDa protein/Snu13 (83, 94), while box H/ACA snoRNAs bind to the pseudouridine synthase dyskerin/Cbf5 (46, 92) and Gar1 (26), Nop10 (28), and Nhp2 (27,28,92). The association of core C/D or H/ACA RNP proteins is essential for the stability and/or proper nucleolar targeting of the snoRNAs (28,46,(91)(92)(93).…”

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confidence: 99%

Identification of Genes That Function in the Biogenesis and Localization of Small Nucleolar RNAs in Saccharomyces cerevisiae

Qiu

Eifert

Wacheul

et al. 2008

Molecular and Cellular Biology

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Small nucleolar RNAs (snoRNAs) orchestrate the modification and cleavage of pre-rRNA and are essential for ribosome biogenesis. Recent data suggest that after nucleoplasmic synthesis, snoRNAs transiently localize to the Cajal body (in plant and animal cells) or the homologous nucleolar body (in budding yeast) for maturation and assembly into snoRNPs prior to accumulation in their primary functional site, the nucleolus. However, little is known about the trans-acting factors important for the intranuclear trafficking and nucleolar localization of snoRNAs. Here, we describe a large-scale genetic screen to identify proteins important for snoRNA transport in Saccharomyces cerevisiae. We performed fluorescence in situ hybridization analysis to visualize U3 snoRNA localization in a collection of temperature-sensitive yeast mutants. We have identified Nop4, Prp21, Tao3, Sec14, and Htl1 as proteins important for the proper localization of U3 snoRNA. Mutations in genes encoding these proteins lead to specific defects in the targeting or retention of the snoRNA to either the nucleolar body or the nucleolus. Additional characterization of the mutants revealed impairment in specific steps of U3 snoRNA processing, demonstrating that snoRNA maturation and trafficking are linked processes.After synthesis in the nucleus, all RNA species undergo a series of maturation steps and transport from the site of synthesis to the site of action, and it is increasingly clear that RNA biogenesis and trafficking are closely linked (54). Whether they are destined to function in the cytoplasm (e.g., rRNA, tRNA, mRNA) or the nucleus (e.g., snRNAs or snoRNAs), all RNAs undergo intranuclear trafficking. It is well established that interactions between trans-acting factors and specific features of RNA substrates can govern which transport pathways will be utilized (38,59,73). However, little is known about the intranuclear trafficking factors and how they affect the molecular movement of RNAs within the nucleus.Small nucleolar RNAs (snoRNAs) provide excellent models to study intranuclear RNA transport. snoRNAs remain within the nucleus, where they undergo biogenesis including covalent alterations (e.g., 5Ј cap hypermethylation and 3Ј-end processing), as well as assembly with specific proteins into stable and functional RNP complexes (snoRNPs) (40,54,70,84). Ultimately, snoRNAs are targeted to nucleoli, where they function in rRNA maturation.The numerous snoRNA species fall into two structurally and functionally distinct classes called the box C/D and box H/ACA snoRNAs (40,54,70,84). Species of both RNA classes interact with pre-rRNA (via base pairing), mainly to guide site-specific nucleotide modification. The majority of box C/D snoRNAs orchestrate 2Ј-O-methylation (12,41,65,89), while the bulk of the box H/ACA RNA species guide pseudouridylation (21, 64). A few RNAs of both classes (e.g., box C/D snoRNA U3 and box H/ACA snoRNA U17 [vertebrates]/snR30 [yeast]) are critical for promoting specific endonucleolytic cleavages of pre-rRNA transcripts ...

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Characterization of the sequences encoding for Xenopus laevis box C/D snoRNP Nop56 protein

Cited by 4 publications

References 13 publications

A nop56 Zebrafish Loss-of-Function Model Exhibits a Severe Neurodegenerative Phenotype

A nop56 Zebrafish Loss-of-Function Model Exhibits a Severe Neurodegenerative Phenotype

Large-scale purification and crystallization of the endoribonuclease XendoU: troubleshooting with His-tagged proteins

Identification of Genes That Function in the Biogenesis and Localization of Small Nucleolar RNAs in Saccharomyces cerevisiae

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