Evidence map›Paper›PMID 16456033›Full record

ArticleNucleic acids research2006

Crystal structure determination and site-directed mutagenesis of the Pyrococcus abyssi aCBF5-aNOP10 complex reveal crucial roles of the C-terminal domains of both proteins in H/ACA sRNP activity.

Xavier Manival, Christophe Charron, Jean-Baptiste Fourmann, François Godard, Bruno Charpentier, Christiane Branlant

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
5.2field-weighted citation impact, top 4% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

42 citing papers in PubMed, 71 citations in OpenAlex.

  1. Article
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  4. Article
  5. Structural Biology of Telomerase.Cold Spring Harbor perspectives in biology · 2019
    Review
  6. Post-transcriptional pseudouridylation in mRNA as well as in some major types of noncoding RNAs.Biochimica et biophysica acta. Gene regulatory mechanisms · 2019
    Review
  7. Article
  8. The Role of Noncoding RNA Pseudouridylation in Nuclear Gene Expression Events.Frontiers in bioengineering and biotechnology · 2018
    Review
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  11. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Xavier ManivalLaboratoire de Maturation des ARN et Enzymologie Moléculaire, UMR 7567 UHP-CNRS, Université des Sciences et Techniques Henri Poincaré, Nancy I, 54506 Vandoeuvre-Lès-Nancy cedex, France.
Christophe Charron
Jean-Baptiste Fourmann
François Godard
Bruno Charpentier
Christiane Branlant
Université de Lorraine · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In archaeal rRNAs, the isomerization of uridine into pseudouridine (Psi) is achieved by the H/ACA sRNPs and the minimal set of proteins required for RNA:Psi-synthase activity is the aCBF5-aNOP10 protein pair. The crystal structure of the aCBF5-aNOP10 heterodimer from Pyrococcus abyssi was solved at 2.1 A resolution. In this structure, protein aNOP10 has an extended shape, with a zinc-binding motif at the N-terminus and an alpha-helix at the C-terminus. Both motifs contact the aCBF5 catalytic domain. Although less efficiently as does the full-length aNOP10, the aNOP10 C-terminal domain binds aCBF5 and stimulates the RNA-guided activity. We show that the C-terminal domain of aCBF5 (the PUA domain), which is wrapped by an N-terminal extension of aCBF5, plays a crucial role for aCBF5 binding to the guide sRNA. Addition of this domain in trans partially complement particles assembled with an aCBF5DeltaPUA truncated protein. In the crystal structure, the aCBF5-aNOP10 complex forms two kinds of heterotetramers with parallel and perpendicular orientations of the aNOP10 terminal alpha-helices, respectively. By gel filtration assay, we showed that aNOP10 can dimerize in solution. As both residues Y41 and L48 were needed for dimerization, the dimerization likely takes place by interaction of parallel alpha-helices.

Indexed as

Models, MolecularAmino Acid SequenceArchaeal ProteinsBinding SitesCatalytic DomainCrystallography, X-RayDimerizationIntramolecular TransferasesLeucineMolecular Sequence DataMutagenesis, Site-DirectedProtein Structure, TertiaryPseudouridinePyrococcus abyssiRibonucleoproteins, Small NucleolarRNA, ArchaealArchaeal ProteinsIntramolecular TransferasesLeucinePseudouridineRibonucleoproteins, Small NucleolarRNA, ArchaealRNA, Small NucleolarRNA, Small UntranslatedTyrosineUridine

Identifiers

PMID16456033
PMCPMC1361308
OpenAlexW2013999256

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.