Evidence map›Paper›PMID 20404317›Full record

ArticleThe Journal of biological chemistry2010

Proteins at the polypeptide tunnel exit of the yeast mitochondrial ribosome.

Steffi Gruschke, Kerstin Gröne, Manfred Heublein, Stefanie Hölz, Lars Israel, Axel Imhof, Johannes M Herrmann, Martin Ott

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 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

32 citing papers in PubMed, 68 citations in OpenAlex.

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  14. Plant Mitochondrial Inner Membrane Protein Insertion.International journal of molecular sciences · 2018
    Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Mitochondrial ribosome assembly in health and disease.Cell cycle (Georgetown, Tex.) · 2015
    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

8 authors at 2 institutions in 1 country.

Steffi GruschkeAbteilung Zellbiologie, Technische Universität Kaiserslautern, 67663 Kaiserslautern, Germany.
Kerstin Gröne
Manfred Heublein
Stefanie Hölz
Lars Israel
Axel Imhof
Johannes M Herrmann
Martin Ott
University of Kaiserslautern · DELudwig-Maximilians-Universität München · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Oxidative phosphorylation in mitochondria requires the synthesis of proteins encoded in the mitochondrial DNA. The mitochondrial translation machinery differs significantly from that of the bacterial ancestor of the organelle. This is especially evident from many mitochondria-specific ribosomal proteins. An important site of the ribosome is the polypeptide tunnel exit. Here, nascent chains are exposed to an aqueous environment for the first time. Many biogenesis factors interact with the tunnel exit of pro- and eukaryotic ribosomes to help the newly synthesized proteins to mature. To date, nothing is known about the organization of the tunnel exit of mitochondrial ribosomes. We therefore undertook a comprehensive approach to determine the composition of the yeast mitochondrial ribosomal tunnel exit. Mitochondria contain homologues of the ribosomal proteins located at this site in bacterial ribosomes. Here, we identified proteins located in their proximity by chemical cross-linking and mass spectrometry. Our analysis revealed a complex network of interacting proteins including proteins and protein domains specific to mitochondrial ribosomes. This network includes Mba1, the membrane-bound ribosome receptor of the inner membrane, as well as Mrpl3, Mrpl13, and Mrpl27, which constitute ribosomal proteins exclusively found in mitochondria. This unique architecture of the tunnel exit is presumably an adaptation of the translation system to the specific requirements of the organelle.

Indexed as

Cell MembraneCross-Linking ReagentsCryoelectron MicroscopyDNA, MitochondrialMass SpectrometryMembrane ProteinsMitochondriaMitochondrial ProteinsOxidative StressPeptidesPhosphorylationProtein ConformationProtein Structure, TertiaryRibosomal ProteinsRibosomesSaccharomyces cerevisiaeCross-Linking ReagentsDNA, MitochondrialMBA1 protein, S cerevisiaeMembrane ProteinsMitochondrial Proteinsmitochondrial ribosomal protein YmL27MRPL13 protein, S cerevisiaeMRPL3 protein, S cerevisiaePeptidesRibosomal ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID20404317
PMCPMC2885179
OpenAlexW2070664727

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.