A Dynamic Scaffold of Pre-snoRNP Factors Facilitates Human Box C/D snoRNP Assembly

McKeegan, Kenneth Scott; Debieux, Charles Maurice; Boulon, Séverine; Bertrand, Édouard; Watkins, Nicholas J.

doi:10.1128/mcb.01097-07

Cited by 88 publications

(140 citation statements)

References 54 publications

(98 reference statements)

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“…In the network built by Sardiu and colleagues, NUFIP is shown to be a RPAP3/R2TP/ prefoldin-like complex interactor (Sardiu et al 2008), which is not surprising given that both NUFIP and its yeast homologue, RSA1, where able to bind the R2TP components PIH1D1 (PIH1/Nop17), RUVBL1 (TIP49) and RUVBL2 (TIP48) (McKeegan et al 2007;Boulon et al 2008). In both studies a role for NUFIP and their associated factors in box C/D snoRNP (or even all L7Ae family RNP) biogenesis was proposed.…”

Section: Nufip1mentioning

confidence: 97%

New insights into the biogenesis of nuclear RNA polymerases?This paper is one of a selection of papers published in this special issue entitled “Canadian Society of Biochemistry, Molecular & Cellular Biology 52nd Annual Meeting — Protein Folding: Principles and Diseases” and has undergone the Journal's usual peer review process.

Cloutier

Coulombe

2010

Biochem. Cell Biol.

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More than 30 years of research on nuclear RNA polymerases (RNAP I, II, and III) has uncovered numerous factors that regulate the activity of these enzymes during the transcription reaction. However, very little is known about the machinery that regulates the fate of RNAPs before or after transcription. In particular, the mechanisms of biogenesis of the 3 nuclear RNAPs, which comprise both common and specific subunits, remains mostly uncharacterized and the proteins involved are yet to be discovered. Using protein affinity purification coupled to mass spectrometry (AP-MS), we recently unraveled a high-density interaction network formed by nuclear RNAP subunits from the soluble fraction of human cell extracts. Validation of the dataset using a machine learning approach trained to minimize the rate of false positives and false negatives yielded a highconfidence dataset and uncovered novel interactors that regulate the RNAP II transcription machinery, including a set of proteins we named the RNAP II-associated proteins (RPAPs). One of the RPAPs, RPAP3, is part of an 11-subunit complex we termed the RPAP3/R2TP/prefoldin-like complex. Here, we review the literature on the subunits of this complex, which points to a role in nuclear RNAP biogenesis.

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Section: Nufip1mentioning

confidence: 97%

New insights into the biogenesis of nuclear RNA polymerases?This paper is one of a selection of papers published in this special issue entitled “Canadian Society of Biochemistry, Molecular & Cellular Biology 52nd Annual Meeting — Protein Folding: Principles and Diseases” and has undergone the Journal's usual peer review process.

Cloutier

Coulombe

2010

Biochem. Cell Biol.

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“…It has been shown that Rvbs and Pih1 as well as Nop56 are co-immunoprecipitated with Nop58 in Hela cells (31). In addition, PIH1D1 depletion resulted in significant decrease of box C/D snoRNAs and accumulation of U3 box C/D snoRNA in Cajal body where snoRNPs transit during its maturation process (31). Furthermore, Su et al showed that snoRNA/snoRNP biogenesis involving RuvBL1/pontin is enhanced in breast cancer (54).…”

Section: Potential Role Of R2tp In Tumorigenesis Through Snornp Pathwaymentioning

confidence: 99%

“…is associated with tumorigenesis. It has been shown that Rvbs and Pih1 as well as Nop56 are co-immunoprecipitated with Nop58 in Hela cells (31). In addition, PIH1D1 depletion resulted in significant decrease of box C/D snoRNAs and accumulation of U3 box C/D snoRNA in Cajal body where snoRNPs transit during its maturation process (31).…”

Section: Potential Role Of R2tp In Tumorigenesis Through Snornp Pathwaymentioning

confidence: 99%

“…It has been proposed that the assembly of box C/D snoRNP starts with the interaction between box C/D snoRNA and Snu13/15.5k, followed by the binding of Nop58 and then Nop1/fibrillarin and Nop56 are recruited (28,32). In this process, Nufip/Rsa1 (snoRNP assembly factor) and Rvbs facilitate the assembly of box C/D snoRNP by bridging the interactions of core components of box C/D snoRNP: between 15.5K and both Nop56 and Nop58 (29)(30)(31). Nufip is likely to regulate the interaction between Rvbs and the box C/D core proteins by tightly interacting with 15.5K (30).…”

Section: R2tp Function In Box C/d Snornp Biogenesismentioning

confidence: 99%

“…This modification is essential for the subsequent endonucleotic cleavage and processing of the pre-rRNA to produce mature rRNAs (21,27). The assembly of snoRNP is hierarchical and its proper assembly is essential for both the activity and stability of snoRNP (6,16,17,(28)(29)(30)(31). It has been proposed that the assembly of box C/D snoRNP starts with the interaction between box C/D snoRNA and Snu13/15.5k, followed by the binding of Nop58 and then Nop1/fibrillarin and Nop56 are recruited (28,32).…”

Section: R2tp Function In Box C/d Snornp Biogenesismentioning

confidence: 99%

See 2 more Smart Citations

The R2TP chaperone complex: its involvement in snoRNP assembly and tumorigenesis

Kakihara

Saeki

2014

Biomolecular Concepts

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R2TP was originally identified in yeast Saccharomyces cerevisiae as Hsp90 interacting complex, and is composed of four different proteins: Rvb1, Rvb2, Tah1, and Pih1. This complex is well-conserved in eukaryotes, and is involved in many cellular processes such as snoRNP biogenesis, RNA polymerase assembly, PIKK signaling, and apoptosis. An increasing number of research related to R2TP suggests a linkage of its function with tumorigenesis. In this review, we provide an overview of several recent studies on R2TP that are related to cell proliferation and carcinogenesis, and propose a possible role of R2TP in tumorigenesis through regulating snoRNA/snoRNP biogenesis.

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The box C/D and H/ACA snoRNPs: key players in the modification, processing and the dynamic folding of ribosomal RNA

2011

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Box C/D and H/ACA RNPs are essential ribonucleoprotein particles that are found throughout both eukaryotes [small nucleolar RNPs (snoRNPs)] and archaea [snoRNP-like complexes (sRNPs)]. These complexes catalyze the site-specific pseudouridylation and most of the methylation of ribosomal RNA (rRNA). The numerous modifications, which are clustered in functionally important regions of the rRNA, are important for rRNA folding and ribosome function. The RNA component of the complexes [small nucleolar RNA (snoRNA) or small RNA (sRNA)] functions in substrate binding by base pairing with the target site and as a scaffold coordinating the organization of the complex. In eukaryotes, a subset of snoRNPs do not catalyze modification but, through base pairing to the rRNA or flanking precursor sequences, direct pre-rRNA folding and are essential for rRNA processing. In the last few years there have been significant advances in our understanding of the structure of archaeal sRNPs. High resolution structures of the archaeal C/D and H/ACA sRNPs have not only provided a detailed understanding of the molecular architecture of these complexes but also produced key insights into substrate binding and product release. In both cases, this is mediated by significant movement in the complexes. Advances have also been made in our knowledge of snoRNP recruitment and release from pre-ribosome complexes in eukaryotes. New snoRNA-rRNA interactions have been documented, and the roles of RNA helicases in releasing snoRNP complexes from the rRNA have been described.

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A Dynamic Scaffold of Pre-snoRNP Factors Facilitates Human Box C/D snoRNP Assembly

Cited by 88 publications

References 54 publications

The R2TP chaperone complex: its involvement in snoRNP assembly and tumorigenesis

The box C/D and H/ACA snoRNPs: key players in the modification, processing and the dynamic folding of ribosomal RNA

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