Evidence map›Paper›PMID 31819999›Full record

ArticleNucleic acids research2020

Composition and processing activity of a semi-recombinant holo U7 snRNP.

Katarzyna Bucholc, Wei Shen Aik, Xiao-Cui Yang, Kaituo Wang, Z Hong Zhou, Michał Dadlez, William F Marzluff, Liang Tong, Zbigniew Dominski

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
0.7field-weighted citation impact, top 30% 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

15 citing papers in PubMed, 18 citations in OpenAlex.

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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

9 authors at 4 institutions in 2 countries.

Katarzyna BucholcIntegrative Program for Biological and Genome Sciences, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.
Wei Shen AikDepartment of Biological Sciences, Columbia University, New York, NY 10027, USA.
Xiao-Cui YangIntegrative Program for Biological and Genome Sciences, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.
Kaituo WangCalifornia NanoSystems Institute, University of California Los Angeles, Los Angeles, CA 90095, USA.
Z Hong ZhouCalifornia NanoSystems Institute, University of California Los Angeles, Los Angeles, CA 90095, USA.
Michał DadlezDepartment of Biophysics, Institute of Biochemistry and Biophysics, Polish Academy of Sciences, 02-106 Warsaw, Poland.
William F MarzluffIntegrative Program for Biological and Genome Sciences, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.
Liang TongDepartment of Biological Sciences, Columbia University, New York, NY 10027, USA.
Zbigniew DominskiIntegrative Program for Biological and Genome Sciences, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.
University of North Carolina at Chapel Hill · USCalifornia NanoSystems Institute · USColumbia University · USInstitute of Biochemistry and Biophysics, Polish Academy of Sciences · PL

Funding

CONTROL OF HISTONE MRNA SYNTHESISR01GM029832 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI DOMINSKI, ZBIGNIEW, MARZLUFF, WILLIAM F. · 1985 to 2022
$9.0M
Structural and functional studies of mRNA processing, stability and quality controlR35GM118093 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI LIANG TONG · 2016 to 2026
$8.5M
NIGMS NIH HHS R01 GM029832NIGMS NIH HHS R35 GM118093
6 · The paper itself

Abstract

In animal cells, replication-dependent histone pre-mRNAs are cleaved at the 3' end by U7 snRNP consisting of two core components: a ∼60-nucleotide U7 snRNA and a ring of seven proteins, with Lsm10 and Lsm11 replacing the spliceosomal SmD1 and SmD2. Lsm11 interacts with FLASH and together they recruit the endonuclease CPSF73 and other polyadenylation factors, forming catalytically active holo U7 snRNP. Here, we assembled core U7 snRNP bound to FLASH from recombinant components and analyzed its appearance by electron microscopy and ability to support histone pre-mRNA processing in the presence of polyadenylation factors from nuclear extracts. We demonstrate that semi-recombinant holo U7 snRNP reconstituted in this manner has the same composition and functional properties as endogenous U7 snRNP, and accurately cleaves histone pre-mRNAs in a reconstituted in vitro processing reaction. We also demonstrate that the U7-specific Sm ring assembles efficiently in vitro on a spliceosomal Sm site but the engineered U7 snRNP is functionally impaired. This approach offers a unique opportunity to study the importance of various regions in the Sm proteins and U7 snRNA in 3' end processing of histone pre-mRNAs.

Indexed as

Amino Acid SequenceAnimalsApoptosis Regulatory ProteinsCalcium-Binding ProteinsCell NucleusDrosophilaHistonesHumansMicemRNA Cleavage and Polyadenylation FactorsProtein BindingRibonucleoproteins, Small NuclearRibonucleoprotein, U7 Small NuclearRNA-Binding ProteinsRNA PrecursorsSpliceosomesApoptosis Regulatory ProteinsCalcium-Binding ProteinsCASP8AP2 protein, humanHistonesLSM10 protein, humanLSM11 protein, humanmRNA Cleavage and Polyadenylation FactorsRibonucleoproteins, Small NuclearRibonucleoprotein, U7 Small NuclearRNA-Binding ProteinsRNA Precursors

Identifiers

PMID31819999
PMCPMC7026596
OpenAlexW2995248179

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.