Evidence map›Paper›PMID 19482034›Full record

ArticleJournal of molecular biology2009

RNA chaperones stimulate formation and yield of the U3 snoRNA-Pre-rRNA duplexes needed for eukaryotic ribosome biogenesis.

Tímea Gérczei, Binal N Shah, Anthony J Manzo, Nils G Walter, Carl C Correll

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

18 citing papers in PubMed, 27 citations in OpenAlex.

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  15. Inside the 40S ribosome assembly machinery.Current opinion in chemical biology · 2011
    Review
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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

5 authors at 2 institutions in 1 country.

Tímea GérczeiDepartment of Biochemistry and Molecular Biology, Rosalind Franklin University of Medicine and Science, North Chicago, IL 60064, USA.
Binal N Shah
Anthony J Manzo
Nils G Walter
Carl C Correll
Rosalind Franklin University of Medicine and Science · USUniversity of Michigan–Ann Arbor · US

Funding

U-turn of the Hepatitis Delta Virus RibozymeR01GM062357 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI WALTER, NILS G · 2001 to 2019
$5.8M
Structure and function of the U3 RNA-protein complexR01GM070491 · NIGMS · ROSALIND FRANKLIN UNIV OF MEDICINE & SCI · PI CORRELL, CARL C · 2007 to 2010
$1.2M
NIGMS NIH HHS GM062357NIGMS NIH HHS GM070491NIGMS NIH HHS R01 GM062357NIGMS NIH HHS R01 GM070491
6 · The paper itself

Abstract

Short duplexes between the U3 small nucleolar RNA and the precursor ribosomal RNA must form quickly and with high yield to satisfy the high demand for ribosome synthesis in rapidly growing eukaryotic cells. These interactions, designated the U3-ETS (external transcribed spacer) and U3-18S duplexes, are essential to initiate the processing of small subunit ribosomal RNA. Previously, we showed that duplexes corresponding to those in Saccharomyces cerevisiae are only observed in vitro after addition of one of two proteins: Imp3p or Imp4p. Here, we used fluorescence-based and other in vitro assays to determine whether these proteins possess RNA chaperone activities and to assess whether these activities are sufficient to satisfy the duplex yield and rate requirements expected in vivo. Assembly of both proteins with the U3 small nucleolar RNA into a chaperone complex destabilizes a U3 stem structure, apparently to expose its 18S base-pairing site. As a result, the chaperone complex accelerates formation of the U3-18S duplex from an undetectable rate to one comparable with the intrinsic rate observed for hybridizing short duplexes. The chaperone complex also stabilizes the U3-ETS duplex by 2.7 kcal/mol. These chaperone activities provide high U3-ETS duplex yield and rapid U3-18S duplex formation over a broad concentration range to help ensure that the U3-precursor ribosomal RNA interactions limit neither ribosome biogenesis nor rapid cell growth. The thermodynamic and kinetic framework used is general and thus suitable for investigating the mechanism of action of other RNA chaperones.

Indexed as

Nucleic Acid ConformationBiological AssayEukaryotic CellsFluorescence Resonance Energy TransferKineticsMolecular ChaperonesNucleic Acid HybridizationRibosomal ProteinsRibosomesRNA PrecursorsRNA, Small NucleolarRNA StabilitySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsThermodynamicsIMP3 protein, S cerevisiaeIMP4 protein, S cerevisiaeMolecular ChaperonesRibosomal ProteinsRNA PrecursorsRNA, Small NucleolarRNA, U3 small nucleolarSaccharomyces cerevisiae Proteins

Identifiers

PMID19482034
PMCPMC2881153
OpenAlexW2128910268

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.