Evidence map›Paper›PMID 27532773›Full record

ArticleeLife2016

Role of Nfu1 and Bol3 in iron-sulfur cluster transfer to mitochondrial clients.

Andrew Melber, Un Na, Ajay Vashisht, Benjamin D Weiler, Roland Lill, James A Wohlschlegel, Dennis R Winge

Open access · goldAbstract read
In one paragraph

Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.

0numbers the graph read from it
0cells of the map it votes in
70citing papers in PubMed
5.8field-weighted citation impact, top 4% 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

70 citing papers in PubMed, 124 citations in OpenAlex.

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  20. Sulfur Administration in Fe-S Cluster Homeostasis.Antioxidants (Basel, Switzerland) · 2021
    Review

10 more citing papers are in PubMed but not listed here.

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

7 authors at 3 institutions in 2 countries.

Andrew MelberDepartment of Medicine, University of Utah Health Sciences Center, Salt Lake City, United States.
Un NaDepartment of Medicine, University of Utah Health Sciences Center, Salt Lake City, United States.
Ajay VashishtDepartment of Biological Chemistry, David Geffen School of Medicine at UCLA, Los Angeles, United States.
Benjamin D WeilerInstitut für Zytobiologie, Philipps-Universität Marburg, Marburg, Germany.
Roland LillInstitut für Zytobiologie, Philipps-Universität Marburg, Marburg, Germany.ORCID 0000-0002-8345-6518
James A WohlschlegelDepartment of Biological Chemistry, David Geffen School of Medicine at UCLA, Los Angeles, United States.
Dennis R WingeDepartment of Medicine, University of Utah Health Sciences Center, Salt Lake City, United States.ORCID 0000-0003-1160-1189
University of Utah · USPhilipps University of Marburg · DEUniversity of California, Los Angeles · US

Funding

UTAH REGIONAL CANCER CENTERP30CA042014 · NCI · UTAH STATE HIGHER EDUCATION SYSTEM--UNIVERSITY OF UTAH · PI KATHARINE S ULLMAN · 1986 to 2026
$72.6M
RESEARCH TRAINING IN HEMATOLOGYT32DK007115 · NIDDK · UNIVERSITY OF UTAH · PI LEIBOLD, ELIZABETH ANN, PRCHAL, JOSEF T · 1986 to 2020
$8.4M
Proteolytic Control of Iron Metabolism by the Ubiquitin Ligase FBXL5R01GM089778 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI WOHLSCHLEGEL, JAMES AKIRA · 2010 to 2023
$4.0M
Succinate Dehydrogenase: Biogenesis and Role in DiseaseR01GM110755 · NIGMS · UNIVERSITY OF UTAH · PI WINGE, DENNIS R. · 2014 to 2021
$2.3M
Biogenesis of Extramitochondrial Iron-Sulfur Proteins in EukaryotesR01GM112763 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI WOHLSCHLEGEL, JAMES AKIRA · 2015 to 2018
$982k
NCI NIH HHS P30 CA042014NIDDK NIH HHS T32 DK007115NIGMS NIH HHS R01 GM089778NIGMS NIH HHS R01 GM110755NIGMS NIH HHS R01 GM112763
6 · The paper itself

Abstract

Iron-sulfur (Fe-S) clusters are essential for many cellular processes, ranging from aerobic respiration, metabolite biosynthesis, ribosome assembly and DNA repair. Mutations in NFU1 and BOLA3 have been linked to genetic diseases with defects in mitochondrial Fe-S centers. Through genetic studies in yeast, we demonstrate that Nfu1 functions in a late step of [4Fe-4S] cluster biogenesis that is of heightened importance during oxidative metabolism. Proteomic studies revealed Nfu1 physical interacts with components of the ISA [4Fe-4S] assembly complex and client proteins that need [4Fe-4S] clusters to function. Additional studies focused on the mitochondrial BolA proteins, Bol1 and Bol3 (yeast homolog to human BOLA3), revealing that Bol1 functions earlier in Fe-S biogenesis with the monothiol glutaredoxin, Grx5, and Bol3 functions late with Nfu1. Given these observations, we propose that Nfu1, assisted by Bol3, functions to facilitate Fe-S transfer from the biosynthetic apparatus to the client proteins preventing oxidative damage to [4Fe-4S] clusters.

Indexed as

Biological TransportIron-Sulfur ProteinsMitochondriaMitochondrial ProteinsProteomeSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsBol1 protein, S cerevisiaeBol3 protein, S cerevisiaeIron-Sulfur ProteinsMitochondrial ProteinsNFU1 protein, S cerevisiaeProteomeSaccharomyces cerevisiae Proteinsbiochemistrycofactor biogenesisiron-sulfur biogenesisiron-sulfur clustersmitochondriaoxidative damageS. cerevisiae

Identifiers

PMID27532773
PMCPMC5014551
OpenAlexW2517099392

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.