Evidence map›Paper›PMID 21610694›Full record

ArticleThe EMBO journal2011

Presequence-dependent folding ensures MrpL32 processing by the m-AAA protease in mitochondria.

Florian Bonn, Takashi Tatsuta, Carmelina Petrungaro, Jan Riemer, Thomas Langer

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
4.0field-weighted citation impact, top 5% 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

40 citing papers in PubMed, 82 citations in OpenAlex.

  1. Molecular mechanisms of mitochondrial AAA+ proteases.The Journal of biological chemistry · 2026
    Review
  2. Recognition of small Tim chaperones by the mitochondrial Yme1 protease.Protein science : a publication of the Protein Society · 2026
    Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Methods to Study the Biogenesis of Mitoribosomal Proteins in Yeast.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  8. Article
  9. Article
  10. Altered Mitochondrial Protein Homeostasis and Proteinopathies.Frontiers in molecular neuroscience · 2022
    Review
  11. Review
  12. Article
  13. Article
  14. Proteolytic Control of Lipid Metabolism.ACS chemical biology · 2019
    Review
  15. Review
  16. Review
  17. Article
  18. Article
  19. Review
  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

5 authors at 2 institutions in 1 country.

Florian BonnInstitute for Genetics, Center for Molecular Medicine (CMMC), Cologne Excellence Cluster on Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of Cologne, Cologne, Germany.
Takashi Tatsuta
Carmelina Petrungaro
Jan Riemer
Thomas Langer
University of Cologne · DEUniversity of Kaiserslautern · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

m-AAA proteases exert dual functions in the mitochondrial inner membrane: they mediate the processing of specific regulatory proteins and ensure protein quality control degrading misfolded polypeptides to peptides. Loss of these activities leads to neuronal cell death in several neurodegenerative disorders. However, it is unclear how the m-AAA protease chooses between specific processing and complete degradation. A central and conserved function of the m-AAA protease is the processing of the ribosomal subunit MrpL32, which regulates ribosome biogenesis and the formation of respiratory complexes. Here, we demonstrate that the formation of a tightly folded domain harbouring a conserved CxxC-X(9)-CxxC sequence motif halts degradation initiated from the N-terminus and triggers the release of mature MrpL32. Oxidative stress impairs folding of MrpL32, resulting in its degradation by the m-AAA protease and decreased mitochondrial translation. Surprisingly, MrpL32 folding depends on its mitochondrial targeting sequence. Presequence-assisted folding of MrpL32 requires the complete import of the MrpL32 precursor before maturation occurs and therefore explains the need for post-translocational processing by the m-AAA protease rather than co-translocational cleavage by the general mitochondrial processing peptidase.

Indexed as

Protein FoldingAmino Acid SequenceCatalytic DomainDeinococcusMetalloendopeptidasesMitochondriaModels, BiologicalModels, MolecularMolecular Sequence DataOrganisms, Genetically ModifiedProtein BindingProtein Processing, Post-TranslationalProtein TransportRibosomal ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae Proteinsm-AAA proteasesMetalloendopeptidasesMrpL32 protein, S cerevisiaeRibosomal ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID21610694
PMCPMC3155303
OpenAlexW1816495367

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.