Evidence map›Paper›PMID 26195779›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2015

Mitochondrial genomes are retained by selective constraints on protein targeting.

Patrik Björkholm, Ajith Harish, Erik Hagström, Andreas M Ernst, Siv G E Andersson

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
4.1field-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

52 citing papers in PubMed, 108 citations in OpenAlex.

  1. Article
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  4. Mitochondrial Genome ofAnimals : an open access journal from MDPI · 2026
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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 2 countries.

Patrik BjörkholmDepartment of Molecular Evolution, Cell, and Molecular Biology, Uppsala University, 752 36 Uppsala, Sweden;
Ajith HarishDepartment of Molecular Evolution, Cell, and Molecular Biology, Uppsala University, 752 36 Uppsala, Sweden;
Erik HagströmDepartment of Molecular Evolution, Cell, and Molecular Biology, Uppsala University, 752 36 Uppsala, Sweden;
Andreas M ErnstDepartment of Cell Biology, Yale University School of Medicine, New Haven, CT 06520.
Siv G E AnderssonDepartment of Molecular Evolution, Cell, and Molecular Biology, Uppsala University, 752 36 Uppsala, Sweden; Siv.Andersson@icm.uu.se.
Uppsala University · SEYale University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mitochondria are energy-producing organelles in eukaryotic cells considered to be of bacterial origin. The mitochondrial genome has evolved under selection for minimization of gene content, yet it is not known why not all mitochondrial genes have been transferred to the nuclear genome. Here, we predict that hydrophobic membrane proteins encoded by the mitochondrial genomes would be recognized by the signal recognition particle and targeted to the endoplasmic reticulum if they were nuclear-encoded and translated in the cytoplasm. Expression of the mitochondrially encoded proteins Cytochrome oxidase subunit 1, Apocytochrome b, and ATP synthase subunit 6 in the cytoplasm of HeLa cells confirms export to the endoplasmic reticulum. To examine the extent to which the mitochondrial proteome is driven by selective constraints within the eukaryotic cell, we investigated the occurrence of mitochondrial protein domains in bacteria and eukaryotes. The accessory protein domains of the oxidative phosphorylation system are unique to mitochondria, indicating the evolution of new protein folds. Most of the identified domains in the accessory proteins of the ribosome are also found in eukaryotic proteins of other functions and locations. Overall, one-third of the protein domains identified in mitochondrial proteins are only rarely found in bacteria. We conclude that the mitochondrial genome has been maintained to ensure the correct localization of highly hydrophobic membrane proteins. Taken together, the results suggest that selective constraints on the eukaryotic cell have played a major role in modulating the evolution of the mitochondrial genome and proteome.

Indexed as

Bacterial ProteinsCell NucleusChloroplast ProteinsComputational BiologyCytochromes bCytosolEndoplasmic ReticulumGenome, MitochondrialHeLa CellsHumansHydrophobic and Hydrophilic InteractionsMembrane ProteinsMitochondrial ProteinsMitochondrial Proton-Translocating ATPasesOxidative PhosphorylationPhylogenyATP synthase subunit 6Bacterial ProteinsChloroplast ProteinsCytochromes bMembrane ProteinsMitochondrial ProteinsMitochondrial Proton-Translocating ATPasesSignal Recognition Particleendoplasmatic reticulumevolutionmitochondriaprotein domainsignal recognition particle

Identifiers

PMID26195779
PMCPMC4547212
OpenAlexW2154304918

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.