Box H/ACA Small Ribonucleoproteins

Kiss, Tamás; Fayet-Lebaron, Eléonore; Jády, Beáta E.

doi:10.1016/j.molcel.2010.01.032

Cited by 223 publications

(227 citation statements)

References 89 publications

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“…Accessory proteins are required to bind its target RNA and trigger its enzymatic activity [30]. Although the main function of H/ACA RNPs is w synthase activity [29], these proteins also participate in specific cleavage of the precursor to 18S rRNA, and dyskerin is also needed for the normal function of the telomerase RNP and telomere maintenance [31]. The main characteristics of PUA domains, their biological functions and architecture were last reviewed in 2007 [9].…”

Section: Introductionmentioning

confidence: 99%

Protein universe containing a PUA RNA‐binding domain

2013

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Here, we review current knowledge about pseudouridine synthase and archaeosine transglycosylase (PUA)‐domain‐containing proteins to illustrate progress in this field. A methodological analysis of the literature about the topic was carried out, together with a ‘qualitative comparative analysis’ to give a more comprehensive review. Bioinformatics methods for whole‐protein or protein‐domain identification are commonly based on pairwise protein sequence comparisons; we added comparison of structures to detect the whole universe of proteins containing the PUA domain. We present an update of proteins having this domain, focusing on the specific proteins present in Homo sapiens (dyskerin, MCT1, Nip7, eIF2D and Nsun6), and explore the existence of these in other species. We also analyze the phylogenetic distribution of the PUA domain in different species and proteins. Finally, we performed a structural comparison of the PUA domain through data mining of structural databases, determining a conserved structural motif, despite the differences in the sequence, even among eukaryotes, archaea and bacteria. All data discussed in this review, both bibliographic and analytical, corroborate the functional importance of the PUA domain in RNA‐binding proteins.

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Section: Introductionmentioning

confidence: 99%

Protein universe containing a PUA RNA‐binding domain

2013

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“…Box H/ACA ribonucleoprotein particles (RNPs) are ancient molecular machines conserved in archaea and eukaryotes that function mainly to convert uridine (U) into pseudouridine (C) post-transcriptionally at specific sites of rRNAs and snRNAs (Meier 2005;Matera et al 2007;Kiss et al 2010). Some special eukaryotic H/ACA RNPs assume functions other than modification.…”

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confidence: 99%

Reconstitution and structural analysis of the yeast box H/ACA RNA-guided pseudouridine synthase

Li¹,

Duan²,

Li³

et al. 2011

Genes Dev.

150

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Box H/ACA ribonucleoprotein particles (RNPs) mediate pseudouridine synthesis, ribosome formation, and telomere maintenance. The structure of eukaryotic H/ACA RNPs remains poorly understood. We reconstituted functional Saccharomyces cerevisiae H/ACA RNPs with recombinant proteins Cbf5, Nop10, Gar1, and Nhp2 and a two-hairpin H/ACA RNA; determined the crystal structure of a Cbf5, Nop10, and Gar1 ternary complex at 1.9 Å resolution; and analyzed the structure-function relationship of the yeast complex. Although eukaryotic H/ACA RNAs have a conserved two-hairpin structure, isolated single-hairpin RNAs are also active in guiding pseudouridylation. Nhp2, unlike its archaeal counterpart, is largely dispensable for the activity, reflecting a functional adaptation of eukaryotic H/ACA RNPs to the variable RNA structure that Nhp2 binds. The N-terminal extension of Cbf5, a hot spot for dyskeratosis congenita mutation, forms an extra structural layer on the PUA domain. Gar1 is distinguished from the assembly factor Naf1 by containing a C-terminal extension that controls substrate turnover and the Gar1-Naf1 exchange during H/ACA RNP maturation. Our results reveal significant novel features of eukaryotic H/ACA RNPs.

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“…Site-speciic isomerization of uridine (U) to Ψ (5-ribosyluracil) is irreversibly catalyzed via Ψ synthases. The family of Ψ synthases (PUS) consists of enzymes which can either function independently or those that require H/ACA ribonucleotide complexes [18]. Compared to U, Ψ contains an extra imino group (>C═NH), which serves as an additional hydrogen bond donor, while the carbon-carbon (C─C) glycosidic bond linking the sugar to the base is more stable than the carbon-nitrogen (C─N) found in U.…”

Section: An Overview Of Post-transcriptional Modiications Of Rnamentioning

confidence: 99%

Epitranscriptomics for Biomedical Discovery

Xiong¹,

Heruth²,

Jiang³

et al. 2017

Applications of RNA-Seq and Omics Strategies - From Microorganisms to Human Health

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Epitranscriptomics is a newly burgeoning ield pertaining to the complete delineation and elucidation of chemical modiications of nucleotides found within all classes of RNA that do not involve a change in the ribonucleotide sequence. More than 140 diverse and distinct nucleotide modiications have been identiied in RNA, dwaring the number of nucleotide modiications found in DNA. The majority of epitranscriptomic modiications have been identiied in ribosomal RNA (rRNA), transfer RNA (tRNA), and small nuclear RNA (snRNA). However, in total, the knowledge of the occurrence, and speciically the function, of RNA modiications remains scarce. Recently, the rapid advancement of next-generation sequencing and mass spectrometry technologies have allowed for the identiication and functional characterization of nucleotide modiications in both protein-coding and non-coding RNA on a global, transcriptome scale. In this chapter, we will introduce the concepts of nucleotide modiication, summarize transcriptome-wide RNA modiication mapping techniques, highlight recent studies exploring the functions of RNA modiications and their association to disease, and inally ofer insight into the future progression of epitranscriptomics.

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Box H/ACA Small Ribonucleoproteins

Cited by 223 publications

References 89 publications

Protein universe containing a PUA RNA‐binding domain

Protein universe containing a PUA RNA‐binding domain

Reconstitution and structural analysis of the yeast box H/ACA RNA-guided pseudouridine synthase

Epitranscriptomics for Biomedical Discovery

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