Evidence map›Paper›PMID 15618406›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2005

The splicing of yeast mitochondrial group I and group II introns requires a DEAD-box protein with RNA chaperone function.

Hon-Ren Huang, Claire E Rowe, Sabine Mohr, Yue Jiang, Alan M Lambowitz, Philip S Perlman

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 96 papers.

0numbers the graph read from it
0cells of the map it votes in
96citing papers in PubMed
4.6field-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

96 citing papers in PubMed, 174 citations in OpenAlex.

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  6. Moderate activity of RNA chaperone maximizes the yield of self-spliced pre-RNA in vivo.Proceedings of the National Academy of Sciences of the United States of America · 2022
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  12. Molecular chaperones maximize the native state yield on biological times by driving substrates out of equilibrium.Proceedings of the National Academy of Sciences of the United States of America · 2017
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36 more citing papers are in PubMed but not listed here.

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.

Hon-Ren HuangDepartment of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, TX 75390-9148, USA.
Claire E Rowe
Sabine Mohr
Yue Jiang
Alan M Lambowitz
Philip S Perlman
The University of Texas Southwestern Medical Center · US

Funding

RNA SPLICING IN NEUROSPORA MITOCHONDRIAR01GM037951 · NIGMS · UNIVERSITY OF TEXAS AUSTIN · PI LAMBOWITZ, ALAN M. · 1986 to 2016
$6.6M
GENETIC AND MOLECULAR STUDIES OF RNA SPLICINGR01GM031480 · NIGMS · UNIVERSITY OF TEXAS SW MED CTR/DALLAS · PI BUTOW, RONALD A · 1985 to 2004
$1.8M
INVOLVEMENT OF PROTEINS IN SPLICING GROUP I INTRONSR37GM037951 · NIGMS · UNIVERSITY OF TEXAS AUSTIN · PI LAMBOWITZ, ALAN M. · 1993 to 2002
$1.2M
NIGMS NIH HHS GM 31480NIGMS NIH HHS GM 37951NIGMS NIH HHS R01 GM031480NIGMS NIH HHS R01 GM037951NIGMS NIH HHS R37 GM037951
6 · The paper itself

Abstract

Group I and II introns self-splice in vitro, but require proteins for efficient splicing in vivo, to stabilize the catalytically active RNA structure. Recent studies showed that the splicing of some Neurospora crassa mitochondrial group I introns additionally requires a DEAD-box protein, CYT-19, which acts as an RNA chaperone to resolve nonnative structures formed during RNA folding. Here we show that, in Saccharomyces cerevisiae mitochondria, a related DEAD-box protein, Mss116p, is required for the efficient splicing of all group I and II introns, some RNA end-processing reactions, and translation of a subset of mRNAs, and that all these defects can be partially or completely suppressed by the expression of CYT-19. Results for the aI2 group II intron indicate that Mss116p is needed after binding the intron-encoded maturase, likely for the disruption of stable but inactive RNA structures. Our results suggest that both group I and II introns are prone to kinetic traps in RNA folding in vivo and that the splicing of both types of introns may require DEAD-box proteins that function as RNA chaperones.

Indexed as

Amino Acid MotifsDEAD-box RNA HelicasesIntronsMitochondriaMolecular ChaperonesMutationProtein BiosynthesisRNARNA HelicasesRNA Processing, Post-TranscriptionalSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsDEAD-box RNA HelicasesMolecular ChaperonesMSS116 protein, S cerevisiaeRNARNA HelicasesSaccharomyces cerevisiae Proteins

Identifiers

PMID15618406
PMCPMC544071
OpenAlexW2148016800

What OpenQuestion holds

Textmetadata
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.