Evidence map›Paper›PMID 23345595›Full record

ArticleMolecular biology of the cell2013

Mge1, a nucleotide exchange factor of Hsp70, acts as an oxidative sensor to regulate mitochondrial Hsp70 function.

Adinarayana Marada, Praveen Kumar Allu, Anjaneyulu Murari, BhoomiReddy PullaReddy, Prasad Tammineni, Venkata Ramana Thiriveedi, Jayasree Danduprolu, Naresh Babu V Sepuri

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Article in Molecular biology of the cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.9field-weighted citation impact, top 14% of its field
1 · What the graph read from it

What it found

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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

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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

21 citing papers in PubMed, 44 citations in OpenAlex.

  1. Review
  2. Article
  3. Mechanisms and regulation of the Hsp70 chaperone network.Nature reviews. Molecular cell biology · 2026
    Review
  4. Article
  5. Article
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  7. Article
  8. Mitochondrial chaperones in human health and disease.Free radical biology & medicine · 2022
    Review
  9. Review
  10. Article
  11. Article
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4 · The record

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5 · Who and what money

Authors and funding

8 authors at 1 institution in 1 country.

Adinarayana MaradaDepartment of Biochemistry, School of Life Sciences, University of Hyderabad, Hyderabad 500046, India.
Praveen Kumar Allu
Anjaneyulu Murari
BhoomiReddy PullaReddy
Prasad Tammineni
Venkata Ramana Thiriveedi
Jayasree Danduprolu
Naresh Babu V Sepuri
University of Hyderabad · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Despite the growing evidence of the role of oxidative stress in disease, its molecular mechanism of action remains poorly understood. The yeast Saccharomyces cerevisiae provides a valuable model system in which to elucidate the effects of oxidative stress on mitochondria in higher eukaryotes. Dimeric yeast Mge1, the cochaperone of heat shock protein 70 (Hsp70), is essential for exchanging ATP for ADP on Hsp70 and thus for recycling of Hsp70 for mitochondrial protein import and folding. Here we show an oxidative stress-dependent decrease in Mge1 dimer formation accompanied by a concomitant decrease in Mge1-Hsp70 complex formation in vitro. The Mge1-M155L substitution mutant stabilizes both Mge1 dimer and Mge1-Hsp70 complex formation. Most important, the Mge1-M155L mutant rescues the slow-growth phenomenon associated with the wild-type Mge1 strain in the presence of H2O2 in vivo, stimulation of the ATPase activity of Hsp70, and the protein import defect during oxidative stress in vitro. Furthermore, cross-linking studies reveal that Mge1-Hsp70 complex formation in mitochondria isolated from wild-type Mge1 cells is more susceptible to reactive oxygen species compared with mitochondria from Mge1-M155L cells. This novel oxidative sensor capability of yeast Mge1 might represent an evolutionarily conserved function, given that human recombinant dimeric Mge1 is also sensitive to H2O2.

Indexed as

Amino Acid SequenceHSP70 Heat-Shock ProteinsHydrogen PeroxideMitochondriaMitochondrial Membrane Transport ProteinsMolecular ChaperonesMutationOxidative StressProtein MultimerizationReactive Oxygen SpeciesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence AlignmentGRPEL1 protein, humanHSP70 Heat-Shock ProteinsHydrogen PeroxideMGE1 protein, S cerevisiaeMitochondrial Membrane Transport ProteinsMolecular ChaperonesReactive Oxygen SpeciesSaccharomyces cerevisiae ProteinsSSA3 protein, S cerevisiae

Identifiers

PMID23345595
PMCPMC3596242
OpenAlexW2047454304

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LicenceCC BY-NC-SA
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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.