Evidence map›Paper›PMID 32518066›Full record

ArticleRNA (New York, N.Y.)2020

Molecular basis for the distinct cellular functions of the Lsm1-7 and Lsm2-8 complexes.

Eric J Montemayor, Johanna M Virta, Samuel M Hayes, Yuichiro Nomura, David A Brow, Samuel E Butcher

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.4field-weighted citation impact, top 10% 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

29 citing papers in PubMed, 41 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

6 authors at 1 institution in 1 country.

Eric J MontemayorDepartment of Biochemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, USA.ORCID 0000-0001-7883-7706
Johanna M VirtaDepartment of Biochemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, USA.
Samuel M HayesDepartment of Biochemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, USA.
Yuichiro NomuraDepartment of Biochemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, USA.ORCID 0000-0002-8275-4468
David A BrowDepartment of Biomolecular Chemistry, University of Wisconsin School of Medicine and Public Health, Madison, Wisconsin 53706, USA.ORCID 0000-0002-8028-014X
Samuel E ButcherDepartment of Biochemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, USA.ORCID 0000-0002-3373-6220
University of Wisconsin–Madison · US

Funding

Overall EvaluationP41GM103403 · NIGMS · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2012 to 2017
$14.3M
Biophysical investigations of RNA complexes essential for gene expressionR35GM118131 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI Samuel E Butcher · 2016 to 2026
$5.1M
RNA-based mechanisms in nuclear steps of gene expressionR35GM118075 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI BROW, DAVID A · 2016 to 2025
$3.1M
Pixel Array Detector for X-ray CrystallographyS10RR029205 · NCRR · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2010 to 2010
$1.8M
ACQUISITION OF MASS SPECTROMETER FOR CORE FACILITYS10RR013790 · NCRR · UNIVERSITY OF WISCONSIN MADISON · PI RAINES, RONALD T · 1999 to 1999
–
NCRR NIH HHS S10 RR013790NCRR NIH HHS S10 RR029205NIGMS NIH HHS P41 GM103403NIGMS NIH HHS R35 GM118075NIGMS NIH HHS R35 GM118131
6 · The paper itself

Abstract

Eukaryotes possess eight highly conserved Lsm (like Sm) proteins that assemble into circular, heteroheptameric complexes, bind RNA, and direct a diverse range of biological processes. Among the many essential functions of Lsm proteins, the cytoplasmic Lsm1-7 complex initiates mRNA decay, while the nuclear Lsm2-8 complex acts as a chaperone for U6 spliceosomal RNA. It has been unclear how these complexes perform their distinct functions while differing by only one out of seven subunits. Here, we elucidate the molecular basis for Lsm-RNA recognition and present four high-resolution structures of Lsm complexes bound to RNAs. The structures of Lsm2-8 bound to RNA identify the unique 2',3' cyclic phosphate end of U6 as a prime determinant of specificity. In contrast, the Lsm1-7 complex strongly discriminates against cyclic phosphates and tightly binds to oligouridylate tracts with terminal purines. Lsm5 uniquely recognizes purine bases, explaining its divergent sequence relative to other Lsm subunits. Lsm1-7 loads onto RNA from the 3' end and removal of the Lsm1 carboxy-terminal region allows Lsm1-7 to scan along RNA, suggesting a gated mechanism for accessing internal binding sites. These data reveal the molecular basis for RNA binding by Lsm proteins, a fundamental step in the formation of molecular assemblies that are central to eukaryotic mRNA metabolism.

Indexed as

Binding SitesProtein BindingRibonucleoproteins, Small NuclearRNARNA-Binding ProteinsRNA Cap-Binding ProteinsRNA, MessengerRNA, Small NuclearRNA SplicingRNA StabilitySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSpliceosomesRibonucleoproteins, Small NuclearRNARNA-Binding ProteinsRNA Cap-Binding ProteinsRNA, MessengerRNA, Small NuclearSaccharomyces cerevisiae ProteinsU6 small nuclear RNALsm1–7Lsm2–8RNA binding proteinsU6 snRNAX-ray crystallography

Identifiers

PMID32518066
PMCPMC7491322
OpenAlexW3032997786

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.