Evidence map›Paper›PMID 29020104›Full record

ArticlePloS one2017

The N-terminal domains of FLASH and Lsm11 form a 2:1 heterotrimer for histone pre-mRNA 3'-end processing.

Wei Shen Aik, Min-Han Lin, Dazhi Tan, Ashutosh Tripathy, William F Marzluff, Zbigniew Dominski, Chi-Yuan Chou, Liang Tong

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2017. 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
1.1field-weighted citation impact, top 22% 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, 36 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

8 authors at 3 institutions in 2 countries.

Wei Shen AikDepartment of Biological Sciences, Columbia University, New York, New York, United States of America.
Min-Han LinDepartment of Life Sciences and Institute of Genome Sciences, National Yang-Ming University, Taipei, Taiwan.
Dazhi TanDepartment of Biological Sciences, Columbia University, New York, New York, United States of America.
Ashutosh TripathyDepartment of Biochemistry and Biophysics, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, United States of America.
William F MarzluffDepartment of Biochemistry and Biophysics, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, United States of America.
Zbigniew DominskiDepartment of Biochemistry and Biophysics, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, United States of America.
Chi-Yuan ChouDepartment of Life Sciences and Institute of Genome Sciences, National Yang-Ming University, Taipei, Taiwan.
Liang TongDepartment of Biological Sciences, Columbia University, New York, New York, United States of America.ORCID http://orcid.org/0000-0002-0563-6468
Columbia University · USUniversity of North Carolina at Chapel Hill · USNational Yang Ming Chiao Tung University · TW

Funding

Overall EvaluationP41GM103403 · NIGMS · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2012 to 2017
$14.3M
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
Pixel Array Detector for X-ray CrystallographyS10RR029205 · NCRR · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2010 to 2010
$1.8M
Pilatus 6mS10OD021832 · OD · UNIVERSITY OF CALIFORNIA BERKELEY · PI ADAMS, PAUL DAVID · 2016 to 2016
$980k
Replacement of an aging X-ray diffraction system for protein crystallographyS10OD012018 · OD · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI TONG, LIANG · 2012 to 2012
$405k
NCRR NIH HHS S10 RR029205NIGMS NIH HHS P41 GM103403NIGMS NIH HHS R01 GM029832NIGMS NIH HHS R35 GM118093NIH HHS S10 OD012018NIH HHS S10 OD021832
6 · The paper itself

Abstract

Unlike canonical pre-mRNAs, animal replication-dependent histone pre-mRNAs lack introns and are processed at the 3'-end by a mechanism distinct from cleavage and polyadenylation. They have a 3' stem loop and histone downstream element (HDE) that are recognized by stem-loop binding protein (SLBP) and U7 snRNP, respectively. The N-terminal domain (NTD) of Lsm11, a component of U7 snRNP, interacts with FLASH NTD and these two proteins recruit the histone cleavage complex containing the CPSF-73 endonuclease for the cleavage reaction. Here, we determined crystal structures of FLASH NTD and found that it forms a coiled-coil dimer. Using solution light scattering, we characterized the stoichiometry of the FLASH NTD-Lsm11 NTD complex and found that it is a 2:1 heterotrimer, which is supported by observations from analytical ultracentrifugation and crosslinking.

Indexed as

Protein MultimerizationRNA Processing, Post-TranscriptionalAmino Acid SequenceBiophysical PhenomenaCarrier ProteinsChromatography, GelCrystallography, X-RayCysteineHistonesLightMutationProtein BindingProtein DomainsProtein Structure, SecondaryRNA-Binding ProteinsRNA PrecursorsCarrier ProteinsCysteineHistonesRNA-Binding ProteinsRNA Precursors

Identifiers

PMID29020104
PMCPMC5636114
OpenAlexW2763458497

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.