Evidence map›Paper›PMID 28416111›Full record

ArticleStructure (London, England : 1993)2017

Structural Analysis Reveals Features of Ribosome Assembly Factor Nsa1/WDR74 Important for Localization and Interaction with Rix7/NVL2.

Yu-Hua Lo, Erin M Romes, Monica C Pillon, Mack Sobhany, Robin E Stanley

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

17 citing papers in PubMed, 27 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

5 authors at 2 institutions in 1 country.

Yu-Hua LoSignal Transduction Laboratory, Department of Health and Human Services, National Institute of Environmental Health Sciences, National Institutes of Health, 111 T. W. Alexander Drive, Research Triangle Park, NC 27709, USA.
Erin M RomesSignal Transduction Laboratory, Department of Health and Human Services, National Institute of Environmental Health Sciences, National Institutes of Health, 111 T. W. Alexander Drive, Research Triangle Park, NC 27709, USA.
Monica C PillonSignal Transduction Laboratory, Department of Health and Human Services, National Institute of Environmental Health Sciences, National Institutes of Health, 111 T. W. Alexander Drive, Research Triangle Park, NC 27709, USA.
Mack SobhanySignal Transduction Laboratory, Department of Health and Human Services, National Institute of Environmental Health Sciences, National Institutes of Health, 111 T. W. Alexander Drive, Research Triangle Park, NC 27709, USA.
Robin E StanleySignal Transduction Laboratory, Department of Health and Human Services, National Institute of Environmental Health Sciences, National Institutes of Health, 111 T. W. Alexander Drive, Research Triangle Park, NC 27709, USA. Electronic address: robin.stanley@nih.gov.
National Institutes of Health · USNational Institute of Environmental Health Sciences · US

Funding

Structure and Function of RNA Processing MachinesZIAES103247 · NIEHS · NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES · PI STANLEY, ROBIN · 2015 to 2025
$22.9M
MINOS (Macromolecular Insights on Nucleic acids Optimized by Scattering)R01GM105404 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI TAINER, JOHN A. · 2012 to 2015
$2.1M
A Pixel Array Detector System for Small Angle X-ray ScatteringS10OD018483 · OD · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI CLASSEN, SCOTT · 2014 to 2014
$998k
Intramural NIH HHS ZIA ES103247NIGMS NIH HHS R01 GM105404NIH HHS S10 OD018483
6 · The paper itself

Abstract

Ribosome assembly is a complex process that requires hundreds of essential assembly factors, including Rix7 (NVL2 in mammals) and Nsa1 (WDR74 in mammals). Rix7 is a type II double ring, AAA-ATPase, which is closely related to the well-known Cdc48/p97. Previous studies in Saccharomyces cerevisiae suggest that Rix7 mediates the release of Nsa1 from nucleolar pre-60S particles; however, the underlying mechanisms of this release are unknown. Through multiple structural analyses we show that S. cerevisiae Nsa1 is composed of an N-terminal seven-bladed WD40 domain followed by a lysine-rich C terminus that extends away from the WD40 domain and is required for nucleolar localization. Co-immunoprecipitation assays with the mammalian homologs identified a well-conserved interface within WDR74 that is important for its association with NVL2. We further show that WDR74 associates with the D1 AAA domain of NVL2, which represents a novel mode of binding of a substrate with a type II AAA-ATPase.

Indexed as

Adenosine TriphosphatasesAmino Acid MotifsAnimalsATPases Associated with Diverse Cellular ActivitiesCarrier ProteinsConserved SequenceHumansNuclear ProteinsProtein BindingProtein DomainsProtein TransportRibosomal ProteinsRNA-Binding ProteinsSaccharomyces cerevisiae ProteinsAdenosine TriphosphatasesATPases Associated with Diverse Cellular ActivitiesCarrier ProteinsNsa1 protein, S cerevisiaeNuclear ProteinsNVL protein, humanRibosomal ProteinsRIX7 protein, S cerevisiaeRNA-Binding ProteinsSaccharomyces cerevisiae ProteinsWDR74 protein, humanAAA-ATPasepre-rRNA processingribosome assemblyWD40 domain

Identifiers

PMID28416111
PMCPMC5415421
OpenAlexW2607084506

What OpenQuestion holds

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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.