Noncoding RNAs of the H/ACA Family

Terns, Michael P.; Terns, Rebecca M.

doi:10.1101/sqb.2006.71.034

Cited by 44 publications

(70 citation statements)

References 108 publications

(177 reference statements)

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“…A vast majority of H/ACA RNPs catalyze site-specific conversion of uridine to its C-glycosyl isomer, pseudouridine. In the modification process, H/ACA RNPs employ small noncoding RNAs to guide substrate RNA recognition and four proteins for pseudouridylation (Bortolin et al 1999;Decatur and Fournier 2003;Meier 2006;Terns and Terns 2006). The guide RNA components of H/ACA sRNPs empower them to act on a large number of complicated RNA target sites that would otherwise require numerous protein enzymes of diverse specificities.…”

Section: Introductionmentioning

confidence: 99%

Long-distance placement of substrate RNA by H/ACA proteins

Liang

Kahen²,

Calvin³

et al. 2008

RNA

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The structural basis for accurate placement of substrate RNA by H/ACA proteins is studied using a nonintrusive fluorescence assay. A model substrate RNA containing 2-aminopurine immediately 39 of the uridine targeted for modification produces distinct fluorescence signals that report the substrate's docking status within the enzyme active site. We combined substrate RNA with complete and subcomplexes of H/ACA ribonucleoprotein particles and monitored changes in the substrate conformation. Our results show that each of the three accessory proteins, as well as an active site residue, have distinct effects on substrate conformations, presumably as docking occurs. Interestingly, in some cases these effects are exerted far from the active site. Application of our data to an available structural model of the holoenzyme, enables the functional role of each accessory protein in substrate placement to come into view.

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Section: Introductionmentioning

confidence: 99%

Long-distance placement of substrate RNA by H/ACA proteins

Liang

Kahen²,

Calvin³

et al. 2008

RNA

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“…166 As developed in this hypothesis, introns were derived from non-coding sequences remaining after the transition to the triplet coding system. The large number of non-coding RNA sequences performing regulatory and guide roles [167][168][169][170][171][172] would also have evolved from sequences that were not involved in triplet coding.…”

Section: Evolution Of Trnasmentioning

confidence: 99%

An alternative to the RNA World Hypothesis

Francis

2011

Trends Evol Biol

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The RNA world hypothesis for the origin of life is widely accepted in spite of the complexity of RNA synthesis. An alternative hypothesis is advanced for the origin and evolution of protein and nucleic acid synthesis. From an early stage synthesis of the evolutionary predecessors of nucleic acids and polypeptides was coupled. This evolved into an RNA replication process that used 3'-aminoacyl-NMP monomers (N= pyrimidine or purine) with a singlet coding system in which the four bases coded for glycine, alanine, valine and aspartic acid. Ribosomal protein synthesis (RPS) evolved from coupled replication by using tRNAs and separating fidelity checking and peptide bond formation functions into small and large ribosomal subunits. Continuity was maintained during the transition to the triplet process by using the same catalysts that aminoacylated NMPs to aminoacylate four different bases at the 3' ends of the original tRNAs. Four GNC codons used the central base to designate the same four amino acids that were coded in singlet replication. Triplet-coded protein synthesis had the advantage of producing multiple copies of protein from a single copy of RNA, and eventually replaced protein synthesis via singlet-coded replication. Evolution of the simple triplet-coded process into RPS is described.

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“…Pseudouridylation modifications of these specific non-coding RNA uridine residues are essential for the functioning and biogenesis of mature ribosomes and spliceosomes [63,138,139]. In addition to their integral role in non-coding RNA biogenesis, the H/ACA proteins are telomerase holoenzyme components that bind to the H/ACA motif in TER [54,58,132]. TER binding to the H/ACA proteins, immediately following transcription, is essential for its processing and in vivo stability [24,67,140].…”

Section: H/aca Binding Proteins -Dyskerin Nhp2 Nop10 and Gar1mentioning

confidence: 99%

“…The H/ACA proteins, dyskerin, NOP10, NHP2 and Gar1, play important roles in the biogenesis and maturation of noncoding RNA, including ribosomal RNAs and small nuclear RNAs [63,131,132]. Dyskerin assembles with NOP10 and NHP2, and at a later stage with the localization factor Gar1, into a ribonucleoprotein complex [133,134].…”

Section: H/aca Binding Proteins -Dyskerin Nhp2 Nop10 and Gar1mentioning

confidence: 99%

Genetic Variations in Telomere Maintenance, with Implications on Tissue Renewal Capacity and Chronic Disease Pathologies

Trudeau¹,

Wong²

2010

CPPM

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Premature loss of telomere repeats underlies the pathologies of inherited bone marrow failure syndromes. Over the past decade, researchers have mapped genetic lesions responsible for the accelerated loss of telomere repeats. Haploinsufficiencies in the catalytic core components of the telomere maintenance enzyme telomerase, as well as genetic defects in telomerase holoenzyme components responsible for enzyme stability, have been linked to hematopoietic failure pathologies. Frequencies of these disease-associated alleles in human populations are low. Accordingly, the diseases themselves are rare. On the other hand, single nucleotide polymorphisms of telomerase enzyme components are found with much higher frequencies, with several non-synonymous SNP alleles observed in 2-4% of the general population. Importantly, recent advents of molecular diagnostic techniques have uncovered links between telomere length maintenance deficiencies and an increasing number of pathologies unrelated to the hematopoietic system. In these cases, short telomere length correlates to tissue renewal capacities and predicts clinical progression and disease severity. To the authors of this review, these new discoveries imply that even minor genetic defects in telomere maintenance can culminate in the premature failure of tissue compartments with high renewal rates. In this review, we discuss the biology and molecules of telomere maintenance, and the pathologies associated with an accelerated loss of telomeres, along with their etiologies. We also discuss single nucleotide polymorphisms of key telomerase components and their association with tissue renewal deficiency syndromes and other pathologies. We suggest that inter-individual variability in telomere maintenance capacity could play a significant role in chronic inflammatory diseases, and that this is not yet fully appreciated in the translational research of pharmacogenomics and personalized medicine.

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Noncoding RNAs of the H/ACA Family

Cited by 44 publications

References 108 publications

Long-distance placement of substrate RNA by H/ACA proteins

Long-distance placement of substrate RNA by H/ACA proteins

An alternative to the RNA World Hypothesis

Genetic Variations in Telomere Maintenance, with Implications on Tissue Renewal Capacity and Chronic Disease Pathologies

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