Evidence map›Paper›PMID 18421378›Full record

ArticlePLoS pathogens2008

Identification of a bacterial-like HslVU protease in the mitochondria of Trypanosoma brucei and its role in mitochondrial DNA replication.

Ziyin Li, Megan E Lindsay, Shawn A Motyka, Paul T Englund, Ching C Wang

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

28 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. The HslV Protease fromInternational journal of molecular sciences · 2019
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. A passion for parasites.The Journal of biological chemistry · 2014
    Article
  14. Article
  15. New insights into the molecular mechanisms of mitosis and cytokinesis in trypanosomes.International review of cell and molecular biology · 2014
    Review
  16. Article
  17. Article
  18. Article
  19. The proteasome of malaria parasites: A multi-stage drug target for chemotherapeutic intervention?International journal for parasitology. Drugs and drug resistance · 2012
    Review
  20. 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

5 authors at 2 institutions in 1 country.

Ziyin LiDepartment of Pharmaceutical Chemistry, University of California, San Francisco, California, United States of America.
Megan E Lindsay
Shawn A Motyka
Paul T Englund
Ching C Wang
Johns Hopkins Medicine · USUniversity of California, San Francisco · US

Funding

STRUCTURE AND SYNTHESIS OF DNAR01AI058613 · NIAID · JOHNS HOPKINS UNIVERSITY · PI JENSEN, ROBERT E · 2004 to 2013
$7.4M
REGULATION OF THE DEVELOPMENT OF TRYPANOSOMA BRUCEIR01AI021786 · NIAID · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI WANG, CHING CHUNG · 1985 to 2012
$4.2M
Regulation of the Development of Trypanosoma bruceiR56AI021786 · NIAID · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI WANG, CHING CHUNG · 2009 to 2009
$286k
NIAID NIH HHS R01 AI-021786NIAID NIH HHS R01 AI021786NIAID NIH HHS R01 AI-058613NIAID NIH HHS R01 AI058613NIAID NIH HHS R56 AI021786
6 · The paper itself

Abstract

ATP-dependent protease complexes are present in all living organisms, including the 26S proteasome in eukaryotes, Archaea, and Actinomycetales, and the HslVU protease in eubacteria. The structure of HslVU protease resembles that of the 26S proteasome, and the simultaneous presence of both proteases in one organism was deemed unlikely. However, HslVU homologs have been identified recently in some primordial eukaryotes, though their potential function remains elusive. We characterized the HslVU homolog from Trypanosoma brucei, a eukaryotic protozoan parasite and the causative agent of human sleeping sickness. TbHslVU has ATP-dependent peptidase activity and, like its bacterial counterpart, has essential lysine and N-terminal threonines in the catalytic subunit. By epitope tagging, TbHslVU localizes to mitochondria and is associated with the mitochondrial genome, kinetoplast DNA (kDNA). RNAi of TbHslVU dramatically affects the kDNA by causing over-replication of the minicircle DNA. This leads to defects in kDNA segregation and, subsequently, to continuous network growth to an enormous size. Multiple discrete foci of nicked/gapped minicircles are formed on the periphery of kDNA disc, suggesting a failure in repairing the gaps in the minicircles for kDNA segregation. TbHslVU is a eubacterial protease identified in the mitochondria of a eukaryote. It has a novel function in regulating mitochondrial DNA replication that has never been observed in other organisms.

Indexed as

AnimalsDNA, KinetoplastDNA, MitochondrialDNA ReplicationEndopeptidase ClpEscherichia coli ProteinsGene SilencingIn Situ Hybridization, FluorescenceMitochondriaMolecular Probe TechniquesRNA InterferenceRNA, Small InterferingTrypanosoma brucei bruceiClpYQ protease, E coliDNA, KinetoplastDNA, MitochondrialEndopeptidase ClpEscherichia coli ProteinsRNA, Small Interfering

Identifiers

PMID18421378
PMCPMC2277460
OpenAlexW2054564337

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.