Evidence map›Paper›PMID 34786732›Full record

ArticleThe EMBO journal2022

Widespread use of unconventional targeting signals in mitochondrial ribosome proteins.

Yury S Bykov, Tamara Flohr, Felix Boos, Naama Zung, Johannes M Herrmann, Maya Schuldiner

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.5field-weighted citation impact, top 9% 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

31 citing papers in PubMed, 51 citations in OpenAlex.

  1. Regulation of cellular proteostasis via mitochondrial protein import.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
    Review
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  6. Mitochondrial presequences are more than just address labels.Protein science : a publication of the Protein Society · 2026
    Review
  7. In and out of the mitochondrial intermembrane space.Protein science : a publication of the Protein Society · 2026
    Review
  8. Article
  9. Article
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  18. PAX-Interacting Protein 1 (PTIP) Promotes Apoptosis.Journal of cellular signaling · 2025
    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

6 authors at 2 institutions in 2 countries.

Yury S BykovDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot, Israel.ORCID 0000-0003-2959-4108
Tamara FlohrDivision of Cell Biology, University of Kaiserslautern, Kaiserslautern, Germany.ORCID 0000-0002-8775-7959
Felix BoosDivision of Cell Biology, University of Kaiserslautern, Kaiserslautern, Germany.
Naama ZungDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot, Israel.ORCID 0000-0002-1517-9774
Johannes M HerrmannDivision of Cell Biology, University of Kaiserslautern, Kaiserslautern, Germany.ORCID 0000-0003-2081-4506
Maya SchuldinerDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot, Israel.ORCID 0000-0001-9947-115X
University of Kaiserslautern · DEWeizmann Institute of Science · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mitochondrial ribosomes are complex molecular machines indispensable for respiration. Their assembly involves the import of several dozens of mitochondrial ribosomal proteins (MRPs), encoded in the nuclear genome, into the mitochondrial matrix. Proteomic and structural data as well as computational predictions indicate that up to 25% of yeast MRPs do not have a conventional N-terminal mitochondrial targeting signal (MTS). We experimentally characterized a set of 15 yeast MRPs in vivo and found that five use internal MTSs. Further analysis of a conserved model MRP, Mrp17/bS6m, revealed the identity of the internal targeting signal. Similar to conventional MTS-containing proteins, the internal sequence mediates binding to TOM complexes. The entire sequence of Mrp17 contains positive charges mediating translocation. The fact that these sequence properties could not be reliably predicted by standard methods shows that mitochondrial protein targeting is more versatile than expected. We hypothesize that structural constraints imposed by ribosome assembly interfaces may have disfavored N-terminal presequences and driven the evolution of internal targeting signals in MRPs.

Indexed as

Protein Sorting SignalsAmino Acid MotifsBacterial ProteinsMitochondriaMitochondrial ProteinsMitochondrial RibosomesModels, BiologicalSaccharomyces cerevisiaeSequence Homology, Amino AcidBacterial ProteinsMitochondrial ProteinsProtein Sorting Signalsmitochondriamitochondrial ribosomemitochondrial targeting signaltargetingtranslocation

Identifiers

PMID34786732
PMCPMC8724765
OpenAlexW3213020535

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.