Evidence map›Paper›PMID 20333239›Full record

ArticlePLoS pathogens2010

The essentials of protein import in the degenerate mitochondrion of Entamoeba histolytica.

Pavel Dolezal, Michael J Dagley, Maya Kono, Peter Wolynec, Vladimir A Likić, Jung Hock Foo, Miroslava Sedinová, Jan Tachezy, Anna Bachmann, Iris Bruchhaus and 1 more

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
4.9field-weighted citation impact, top 4% 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

39 citing papers in PubMed, 71 citations in OpenAlex.

  1. Structural insights into interdomain interactions inJournal of structural biology: X · 2026
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  10. Import ofMicroorganisms · 2020
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  11. AnGenes · 2019
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  12. Fe-S cluster assembly in the supergroup Excavata.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018
    Review
  13. Article
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  15. Article
  16. Article
  17. Article
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  19. Diversity and origins of anaerobic metabolism in mitochondria and related organelles.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 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

11 authors at 4 institutions in 3 countries.

Pavel DolezalDepartment of Biochemistry and Molecular Biology, Monash University, Clayton Campus, Melbourne, Victoria, Australia. paveldolezal@yahoo.com
Michael J Dagley
Maya Kono
Peter Wolynec
Vladimir A Likić
Jung Hock Foo
Miroslava Sedinová
Jan Tachezy
Anna Bachmann
Iris Bruchhaus
Trevor Lithgow
Monash University · AUBernhard Nocht Institute for Tropical Medicine · DECharles University · CZUniversity of Melbourne · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Several essential biochemical processes are situated in mitochondria. The metabolic transformation of mitochondria in distinct lineages of eukaryotes created proteomes ranging from thousands of proteins to what appear to be a much simpler scenario. In the case of Entamoeba histolytica, tiny mitochondria known as mitosomes have undergone extreme reduction. Only recently a single complete metabolic pathway of sulfate activation has been identified in these organelles. The E. histolytica mitosomes do not produce ATP needed for the sulfate activation pathway and for three molecular chaperones, Cpn60, Cpn10 and mtHsp70. The already characterized ADP/ATP carrier would thus be essential to provide cytosolic ATP for these processes, but how the equilibrium of inorganic phosphate could be maintained was unknown. Finally, how the mitosomal proteins are translocated to the mitosomes had remained unclear. We used a hidden Markov model (HMM) based search of the E. histolytica genome sequence to discover candidate (i) mitosomal phosphate carrier complementing the activity of the ADP/ATP carrier and (ii) membrane-located components of the protein import machinery that includes the outer membrane translocation channel Tom40 and membrane assembly protein Sam50. Using in vitro and in vivo systems we show that E. histolytica contains a minimalist set up of the core import components in order to accommodate a handful of mitosomal proteins. The anaerobic and parasitic lifestyle of E. histolytica has produced one of the simplest known mitochondrial compartments of all eukaryotes. Comparisons with mitochondria of another amoeba, Dictystelium discoideum, emphasize just how dramatic the reduction of the protein import apparatus was after the loss of archetypal mitochondrial functions in the mitosomes of E. histolytica.

Indexed as

AnimalsCytoplasmic VesiclesEntamoeba histolyticaGenome, ProtozoanMarkov ChainsMitochondriaMitochondrial ProteinsPhosphatesPhosphate Transport ProteinsPhylogenyProtein TransportProtozoan ProteinsSaccharomyces cerevisiaeMitochondrial ProteinsPhosphatesPhosphate Transport ProteinsProtozoan Proteins

Identifiers

PMID20333239
PMCPMC2841616
OpenAlexW2032549722

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.