Evidence map›Paper›PMID 21698192›Full record

ArticlePloS one2011

A histone-like protein of mycobacteria possesses ferritin superfamily protein-like activity and protects against DNA damage by Fenton reaction.

Masaki Takatsuka, Mayuko Osada-Oka, Eisuke F Satoh, Kengo Kitadokoro, Yukiko Nishiuchi, Mamiko Niki, Masayasu Inoue, Kazuhiro Iwai, Tetsuo Arakawa, Yoshihiro Shimoji and 4 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

20 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Iron uptake and transport by the carboxymycobactin-mycobactin siderophore machinery of Mycobacterium tuberculosis is dependent on the iron-regulated protein HupB.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2021
    Article
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  7. Observational
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  13. Article
  14. Metallobiology of Tuberculosis.Microbiology spectrum · 2014
    Review
  15. Article
  16. Article
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  18. Article
  19. Article
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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

14 authors at 7 institutions in 2 countries.

Masaki TakatsukaDepartment of Bacteriology, Osaka City University Graduate School of Medicine, Abeno-ku, Osaka, Japan.
Mayuko Osada-Oka
Eisuke F Satoh
Kengo Kitadokoro
Yukiko Nishiuchi
Mamiko Niki
Masayasu Inoue
Kazuhiro Iwai
Tetsuo Arakawa
Yoshihiro Shimoji
Hisashi Ogura
Kazuo Kobayashi
Anura Rambukkana
Sohkichi Matsumoto
Osaka City University · JPKyoto Institute of Technology · JPNational Institute of Animal Health · JPNational Institute of Infectious Diseases · JPOsaka University · JPToneyama National Hospital · JPUniversity of Edinburgh · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Iron is an essential metal for living organisms but its level must be strictly controlled in cells, because ferrous ion induces toxicity by generating highly active reactive oxygen, hydroxyl radicals, through the Fenton reaction. In addition, ferric ion shows low solubility under physiological conditions. To overcome these obstacles living organisms possess Ferritin superfamily proteins that are distributed in all three domains of life: bacteria, archaea, and eukaryotes. These proteins minimize hydroxyl radical formation by ferroxidase activity that converts Fe(2+) into Fe(3+) and sequesters iron by storing it as a mineral inside a protein cage. In this study, we discovered that mycobacterial DNA-binding protein 1 (MDP1), a histone-like protein, has similar activity to ferritin superfamily proteins. MDP1 prevented the Fenton reaction and protects DNA by the ferroxidase activity. The K(m) values of the ferroxidase activity by MDP1 of Mycobacterium bovis bacillus Calmette-Guérin (BCG-3007c), Mycobacterium tuberculosis (Rv2986c), and Mycobacterium leprae (ML1683; ML-LBP) were 0.292, 0.252, and 0.129 mM, respectively. Furthermore, one MDP1 molecule directly captured 81.4±19.1 iron atoms, suggesting the role of this protein in iron storage. This study describes for the first time a ferroxidase-iron storage protein outside of the ferritin superfamily proteins and the protective role of this bacterial protein from DNA damage.

Indexed as

DNA DamageCeruloplasminFerritinsHistonesMycobacteriumPhylogenyProtein BindingCeruloplasminFerritinsHistones

Identifiers

PMID21698192
PMCPMC3116847
OpenAlexW2082330109

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

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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.