Evidence map›Paper›PMID 26055323›Full record

ArticleMolecular and cellular biology2015

Probing the Biology of Giardia intestinalis Mitosomes Using In Vivo Enzymatic Tagging.

Eva Martincová, Luboš Voleman, Jan Pyrih, Vojtěch Žárský, Pavlína Vondráčková, Martin Kolísko, Jan Tachezy, Pavel Doležal

Abstract read
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Article in Molecular and cellular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
–field-weighted citation impact
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

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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

27 citing papers in PubMed.

  1. Article
  2. Review
  3. Parasitology · 2026
    Review
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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

8 authors.

Eva MartincováDepartment of Parasitology, Faculty of Science, Charles University in Prague, Prague, Czech Republic.
Luboš VolemanDepartment of Parasitology, Faculty of Science, Charles University in Prague, Prague, Czech Republic.
Jan PyrihDepartment of Parasitology, Faculty of Science, Charles University in Prague, Prague, Czech Republic.
Vojtěch ŽárskýDepartment of Parasitology, Faculty of Science, Charles University in Prague, Prague, Czech Republic.
Pavlína VondráčkováDepartment of Parasitology, Faculty of Science, Charles University in Prague, Prague, Czech Republic.
Martin KolískoCentre for Microbial Diversity and Evolution, Department of Botany, University of British Columbia, Vancouver, BC, Canada.
Jan TachezyDepartment of Parasitology, Faculty of Science, Charles University in Prague, Prague, Czech Republic.
Pavel DoležalDepartment of Parasitology, Faculty of Science, Charles University in Prague, Prague, Czech Republic pavel.dolezal@natur.cuni.cz.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Giardia intestinalis parasites contain mitosomes, one of the simplest mitochondrion-related organelles. Strategies to identify the functions of mitosomes have been limited mainly to homology detection, which is not suitable for identifying species-specific proteins and their functions. An in vivo enzymatic tagging technique based on the Escherichia coli biotin ligase (BirA) has been introduced to G. intestinalis; this method allows for the compartment-specific biotinylation of a protein of interest. Known proteins involved in the mitosomal protein import were in vivo tagged, cross-linked, and used to copurify complexes from the outer and inner mitosomal membranes in a single step. New proteins were then identified by mass spectrometry. This approach enabled the identification of highly diverged mitosomal Tim44 (GiTim44), the first known component of the mitosomal inner membrane translocase (TIM). In addition, our subsequent bioinformatics searches returned novel diverged Tim44 paralogs, which mediate the translation and mitosomal insertion of mitochondrially encoded proteins in other eukaryotes. However, most of the identified proteins are specific to G. intestinalis and even absent from the related diplomonad parasite Spironucleus salmonicida, thus reflecting the unique character of the mitosomal metabolism. The in vivo enzymatic tagging also showed that proteins enter the mitosome posttranslationally in an unfolded state and without vesicular transport.

Indexed as

Amino Acid SequenceAnimalsBiotinylationCarbon-Nitrogen LigasesCell FractionationEscherichia coliEscherichia coli ProteinsGiardia lambliaGiardiasisHumansMass SpectrometryModels, MolecularMolecular Sequence DataOrganellesProtozoan ProteinsRepressor ProteinsbirA protein, E coliCarbon-Nitrogen LigasesEscherichia coli ProteinsProtozoan ProteinsRepressor Proteins

Identifiers

PMID26055323
PMCPMC4508323

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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.