Archaeal fibrillarin–Nop5 heterodimer 2′-<i>O</i>-methylates RNA independently of the C/D guide RNP particle

Tomkuvienė, Miglė; Ličytė, Janina; Olendraitė, Ingrida; Liutkevičiūtė, Zita; Clouet‐d’Orval, Béatrice; Klimašauskas, Saulius

doi:10.1261/rna.059832.116

Cited by 6 publications

(6 citation statements)

References 65 publications

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“…Interestingly, depletion of the four snoRNP proteins did not impact rRNA processing but noticeably reduced the frequency of rRNA methylation, which suggests a different assembly mechanism of processing from the methylation snoRNPs (Li et al 2018). Evidence was also found in an archaeal sRNP that fibrillarin and Nop5 complex could have RNP-independent methylation activity through a guidefree target RNA binding model (Tomkuvienė et al 2017). A human snoRNA, SNORD27, regulates E2F7 pre-mRNA alternative splicing by masking splice sites through basepairing.…”

Section: Evidence For Functional Diversity Of C/d Snornpsmentioning

confidence: 99%

The multistructural forms of box C/D ribonucleoprotein particles

Zhao

2018

RNA

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Structural biology studies of archaeal and yeast box C/D ribonucleoprotein particles (RNPs) reveal a surprisingly wide range of forms. If form ever follows function, the different structures of box C/D small ribonucleoprotein particles (snoRNPs) may reflect their versatile functional roles beyond what has been recognized. A large majority of box C/D RNPs serve to site-specifically methylate the ribosomal RNA, typically as independent complexes. Select members of the box C/D snoRNPs also are essential components of the megadalton RNP enzyme, the small subunit processome that is responsible for processing ribosomal RNA. Other box C/D RNPs continue to be uncovered with either unexpected or unknown functions. We summarize currently known box C/D RNP structures in this review and identify the Nop56/58 and box C/D RNA subunits as the key elements underlying the observed structural diversity, and likely, the diverse functional roles of box C/D RNPs.

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Section: Evidence For Functional Diversity Of C/d Snornpsmentioning

confidence: 99%

The multistructural forms of box C/D ribonucleoprotein particles

Zhao

2018

RNA

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“…Indeed, this function is mainly insured by C/D-box s(sno)RNPs. Interestingly, a recent report described a newly discovered stand-alone activity of archaeal Fib-Nop5 heterodimer that can perform 2'-Omethylation of SSU-16S and LSU-23S rRNAs in Pyrococcus abyssi [137].…”

Section: Stand-alone Rrna 2'-o-methyltransferasesmentioning

confidence: 99%

RNA ribose methylation (2′-O-methylation): Occurrence, biosynthesis and biological functions

Ayadi

Galvanin

Pichot

et al. 2019

Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanism

127

116

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Methylation of riboses at 2'-OH group is one of the most common RNA modifications found in number of cellular RNAs from almost any species which belong to all three life domains. This modification was extensively studied for decades in rRNAs and tRNAs, but recent data revealed the presence of 2'-O-methyl groups also in low abundant RNAs, like mRNAs.Ribose methylation is formed in RNA by two alternative enzymatic mechanisms: either by stand-alone protein enzymes or by complex assembly of proteins associated with snoRNA guides (sno(s)RNPs). In that case one catalytic subunit acts at various RNA sites, the specificity is provided by base pairing of the sno(s)RNA guide with the target RNA. In this review we compile available information on 2'-OH ribose methylation in different RNAs, enzymatic machineries involved in their biosynthesis and dynamics, as well as on the physiological functions of these modified residues.

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“…Fibrillarin forms part of one of the main snoRNP complexes that modify rRNA during ribosomal RNA biogenesis; this complex guides the specific methylation site of about 100 residues in the rRNA. The complex consists of three other well-known proteins: Nop58, Nop56, 15.5K, and one snoRNA guide [52][53][54][55].…”

Section: Ribonuclease Activity Of the Recombinant Ribonucleoparticle ...mentioning

confidence: 99%

Fibrillarin Ribonuclease Activity is Dependent on the GAR Domain and Modulated by Phospholipids

Guillén-Chable

Corona

Pereira-Santana

et al. 2020

Cells

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Fibrillarin is a highly conserved nucleolar methyltransferase responsible for ribosomal RNA methylation across evolution from Archaea to humans. It has been reported that fibrillarin is involved in the methylation of histone H2A in nucleoli and other processes, including viral progression, cellular stress, nuclear shape, and cell cycle progression. We show that fibrillarin has an additional activity as a ribonuclease. The activity is affected by phosphoinositides and phosphatidic acid and insensitive to ribonuclease inhibitors. Furthermore, the presence of phosphatidic acid releases the fibrillarin-U3 snoRNA complex. We show that the ribonuclease activity localizes to the GAR (glycine/arginine-rich) domain conserved in a small group of RNA interacting proteins. The introduction of the GAR domain occurred in evolution in the transition from archaea to eukaryotic cells. The interaction of this domain with phospholipids may allow a phase separation of this protein in nucleoli.

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Archaeal fibrillarin–Nop5 heterodimer 2′-O-methylates RNA independently of the C/D guide RNP particle

Cited by 6 publications

References 65 publications

The multistructural forms of box C/D ribonucleoprotein particles

The multistructural forms of box C/D ribonucleoprotein particles

RNA ribose methylation (2′-O-methylation): Occurrence, biosynthesis and biological functions

Fibrillarin Ribonuclease Activity is Dependent on the GAR Domain and Modulated by Phospholipids

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