Evidence map›Paper›PMID 21239625›Full record

ArticleEukaryotic cell2011

Depletion of mitochondrial acyl carrier protein in bloodstream-form Trypanosoma brucei causes a kinetoplast segregation defect.

April M Clayton, Jennifer L Guler, Megan L Povelones, Eva Gluenz, Keith Gull, Terry K Smith, Robert E Jensen, Paul T Englund

Open access · diamondAbstract read
In one paragraph

Article in Eukaryotic cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

13 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Review
  3. Molecular model of the mitochondrial genome segregation machinery inProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Biochemistry and evolution of anaerobic energy metabolism in eukaryotes.Microbiology and molecular biology reviews : MMBR · 2012
    Review
  12. Article
  13. Review
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 4 institutions in 2 countries.

April M ClaytonDepartment of Biological Chemistry, Johns Hopkins University School of Medicine, 725 N. Wolfe St., Baltimore, MD 21205, USA.
Jennifer L Guler
Megan L Povelones
Eva Gluenz
Keith Gull
Terry K Smith
Robert E Jensen
Paul T Englund
Johns Hopkins Medicine · USUniversity of Oxford · GBJohns Hopkins University · USUniversity of St Andrews · GB

Funding

STRUCTURE AND SYNTHESIS OF DNAR01AI058613 · NIAID · JOHNS HOPKINS UNIVERSITY · PI JENSEN, ROBERT E · 2004 to 2013
$7.4M
Trypansome Surface GlycoproteinsR01AI021334 · NIAID · JOHNS HOPKINS UNIVERSITY · PI ENGLUND, PAUL T · 1985 to 2006
$2.8M
MITOCHONDRIAL DYNAMICS-MORPHOLOGY/DIVISION/SEGREGATIONR01GM054021 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI JENSEN, ROBERT E · 1996 to 2008
$2.7M
NIAID NIH HHS AI058613NIAID NIH HHS AI21334NIAID NIH HHS R01 AI021334NIAID NIH HHS R01 AI058613NIGMS NIH HHS GM54021NIGMS NIH HHS R01 GM054021Wellcome TrustWellcome Trust 086658
6 · The paper itself

Abstract

Like other eukaryotes, trypanosomes have an essential type II fatty acid synthase in their mitochondrion. We have investigated the function of this synthase in bloodstream-form parasites by studying the effect of a conditional knockout of acyl carrier protein (ACP), a key player in this fatty acid synthase pathway. We found that ACP depletion not only caused small changes in cellular phospholipids but also, surprisingly, caused changes in the kinetoplast. This structure, which contains the mitochondrial genome in the form of a giant network of several thousand interlocked DNA rings (kinetoplast DNA [kDNA]), became larger in some cells and smaller or absent in others. We observed the same pattern in isolated networks viewed by either fluorescence or electron microscopy. We found that the changes in kDNA size were not due to the disruption of replication but, instead, to a defect in segregation. kDNA segregation is mediated by the tripartite attachment complex (TAC), and we hypothesize that one of the TAC components, a differentiated region of the mitochondrial double membrane, has an altered phospholipid composition when ACP is depleted. We further speculate that this compositional change affects TAC function, and thus kDNA segregation.

Indexed as

Acyl Carrier ProteinBloodDNA, KinetoplastHumansMitochondrial ProteinsProtozoan ProteinsTrypanosoma brucei bruceiTrypanosomiasis, AfricanAcyl Carrier ProteinDNA, KinetoplastMitochondrial ProteinsProtozoan Proteins

Identifiers

PMID21239625
PMCPMC3067480
OpenAlexW2134011693

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.