Evidence map›Paper›PMID 25733880›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2015

Dramatically reduced spliceosome in Cyanidioschyzon merolae.

Martha R Stark, Elizabeth A Dunn, William S C Dunn, Cameron J Grisdale, Anthony R Daniele, Matthew R G Halstead, Naomi M Fast, Stephen D Rader

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
3.8field-weighted citation impact, top 7% 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

33 citing papers in PubMed, 60 citations in OpenAlex.

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  12. A single mNature communications · 2021
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  15. The SF3b complex: splicing and beyond.Cellular and molecular life sciences : CMLS · 2020
    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

8 authors at 2 institutions in 1 country.

Martha R StarkDepartment of Chemistry, University of Northern British Columbia, Prince George, BC, V2N 4Z9 Canada; and.
Elizabeth A DunnDepartments of Biochemistry and Molecular Biology, and.
William S C DunnDepartment of Chemistry, University of Northern British Columbia, Prince George, BC, V2N 4Z9 Canada; and.
Cameron J GrisdaleBotany, University of British Columbia, Vancouver, BC, V6T 1Z4 Canada.
Anthony R DanieleDepartment of Chemistry, University of Northern British Columbia, Prince George, BC, V2N 4Z9 Canada; and.
Matthew R G HalsteadDepartment of Chemistry, University of Northern British Columbia, Prince George, BC, V2N 4Z9 Canada; and.
Naomi M FastBotany, University of British Columbia, Vancouver, BC, V6T 1Z4 Canada.
Stephen D RaderDepartment of Chemistry, University of Northern British Columbia, Prince George, BC, V2N 4Z9 Canada; and Departments of Biochemistry and Molecular Biology, and rader@unbc.ca.ORCID http://orcid.org/0000-0001-7242-1785
University of Northern British Columbia · CAUniversity of British Columbia · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The human spliceosome is a large ribonucleoprotein complex that catalyzes pre-mRNA splicing. It consists of five snRNAs and more than 200 proteins. Because of this complexity, much work has focused on the Saccharomyces cerevisiae spliceosome, viewed as a highly simplified system with fewer than half as many splicing factors as humans. Nevertheless, it has been difficult to ascribe a mechanistic function to individual splicing factors or even to discern which are critical for catalyzing the splicing reaction. We have identified and characterized the splicing machinery from the red alga Cyanidioschyzon merolae, which has been reported to harbor only 26 intron-containing genes. The U2, U4, U5, and U6 snRNAs contain expected conserved sequences and have the ability to adopt secondary structures and form intermolecular base-pairing interactions, as in other organisms. C. merolae has a highly reduced set of 43 identifiable core splicing proteins, compared with ∼90 in budding yeast and ∼140 in humans. Strikingly, we have been unable to find a U1 snRNA candidate or any predicted U1-associated proteins, suggesting that splicing in C. merolae may occur without the U1 small nuclear ribonucleoprotein particle. In addition, based on mapping the identified proteins onto the known splicing cycle, we propose that there is far less compositional variability during splicing in C. merolae than in other organisms. The observed reduction in splicing factors is consistent with the elimination of spliceosomal components that play a peripheral or modulatory role in splicing, presumably retaining those with a more central role in organization and catalysis.

Indexed as

Algal ProteinsBase PairingHumansImmunoprecipitationIntronsModels, BiologicalNucleic Acid ConformationRhodophytaRNA PrecursorsRNA, Small NuclearRNA SplicingRNA StabilitySpliceosomesAlgal ProteinsRNA PrecursorsRNA, Small Nucleargenome reductionpre-mRNA splicingspliceosome coresplicing mechanismU1 snRNP

Identifiers

PMID25733880
PMCPMC4371933
OpenAlexW2150970670

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.