Evidence map›Paper›PMID 20889970›Full record

ArticleThe Journal of biological chemistry2010

Mitochondrial NADH kinase, Pos5p, is required for efficient iron-sulfur cluster biogenesis in Saccharomyces cerevisiae.

Jayashree Pain, M M Balamurali, Andrew Dancis, Debkumar Pain

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

25 citing papers in PubMed, 41 citations in OpenAlex.

  1. Phenomic and Transcriptomic Profiling of ZnS QD Response inNanomaterials (Basel, Switzerland) · 2026
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  5. Mitochondria function in cytoplasmic FeS protein biogenesis.Biochimica et biophysica acta. Molecular cell research · 2024
    Review
  6. Article
  7. Yeast Mitochondria Import Aqueous FeJournal of the American Chemical Society · 2023
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Anilinopyrimidine Resistance inFrontiers in microbiology · 2017
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
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

4 authors at 3 institutions in 1 country.

Jayashree PainDepartment of Pharmacology and Physiology, University of Medicine and Dentistry of New Jersey, New Jersey Medical School, Newark, New Jersey 07101, USA.
M M Balamurali
Andrew Dancis
Debkumar Pain
Rutgers New Jersey Medical SchoolRutgers, The State University of New Jersey · USUniversity of Pennsylvania · US

Funding

Biochemistry and genetics of iron transport in mitochondria and related processesR37DK053953 · NIDDK · UNIVERSITY OF PENNSYLVANIA · PI DANCIS, ANDREW B. · 2008 to 2015
$2.9M
Mitochondrial aconitase: Fe-S cluster biogenesis and interaction with mtDNAR01AG030504 · NIA · UNIV OF MED/DENT OF NJ-NJ MEDICAL SCHOOL · PI PAIN, DEBKUMAR · 2008 to 2012
$1.6M
NIA NIH HHS AG030504NIA NIH HHS R01 AG030504NIDDK NIH HHS R37 DK053953NIDDK NIH HHS R37DK053953
6 · The paper itself

Abstract

In Saccharomyces cerevisiae, the mitochondrial inner membrane readily allows transport of cytosolic NAD(+), but not NADPH, to the matrix. Pos5p is the only known NADH kinase in the mitochondrial matrix. The enzyme phosphorylates NADH to NADPH and is the major source of NADPH in the matrix. The importance of mitochondrial NADPH for cellular physiology is underscored by the phenotypes of the Δpos5 mutant, characterized by oxidative stress sensitivity and iron-sulfur (Fe-S) cluster deficiency. Fe-S clusters are essential cofactors of proteins such as aconitase [4Fe-4S] and ferredoxin [2Fe-2S] in mitochondria. Intact mitochondria isolated from wild-type yeast can synthesize these clusters and insert them into the corresponding apoproteins. Here, we show that this process of Fe-S cluster biogenesis in wild-type mitochondria is greatly stimulated and kinetically favored by the addition of NAD(+) or NADH in a dose-dependent manner, probably via transport into mitochondria and subsequent conversion into NADPH. Unlike wild-type mitochondria, Δpos5 mitochondria cannot efficiently synthesize Fe-S clusters on endogenous aconitase or imported ferredoxin, although cluster biogenesis in isolated Δpos5 mitochondria is restored to a significant extent by a small amount of imported Pos5p. Interestingly, Fe-S cluster biogenesis in wild-type mitochondria is further enhanced by overexpression of Pos5p. The effects of Pos5p on Fe-S cluster generation in mitochondria indicate that one or more steps in the biosynthetic process require NADPH. The role of mitochondrial NADPH in Fe-S cluster biogenesis appears to be distinct from its function in anti-oxidant defense.

Indexed as

Gene Expression Regulation, FungalAconitate HydrataseDose-Response Relationship, DrugFerredoxinsIron-Sulfur ProteinsKineticsMitochondriaMitochondrial ProteinsModels, GeneticNADOxidative StressOxygenPhosphotransferases (Alcohol Group Acceptor)Saccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSulfurAconitate HydrataseFerredoxinsIron-Sulfur ProteinsMitochondrial ProteinsNADOxygenPhosphotransferases (Alcohol Group Acceptor)POS5 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSulfur

Identifiers

PMID20889970
PMCPMC2998133
OpenAlexW2089394565

What OpenQuestion holds

Textmetadata
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.