Evidence map›Paper›PMID 18663012›Full record

ArticleNucleic acids research2008

DNA organization by the apicoplast-targeted bacterial histone-like protein of Plasmodium falciparum.

E V S Raghu Ram, Rangeetha Naik, Munia Ganguli, Saman Habib

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

19 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
  2. mSphere · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. HBD1 protein with a tandem repeat of two HMG-box domains is a DNA clip to organize chloroplast nucleoids inProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Architectural organization in E. coli nucleoid.Biochimica et biophysica acta · 2012
    Review
  14. Article
  15. Article
  16. The apicomplexan plastid and its evolution.Cellular and molecular life sciences : CMLS · 2011
    Review
  17. Article
  18. Article
  19. 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

4 authors at 2 institutions in 1 country.

E V S Raghu RamDivision of Molecular and Structural Biology, Central Drug Research Institute, Lucknow-226 001, India.
Rangeetha Naik
Munia Ganguli
Saman Habib
Central Drug Research Institute · INInstitute of Genomics and Integrative Biology · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Apicomplexans, including the pathogens Plasmodium and Toxoplasma, carry a nonphotosynthetic plastid of secondary endosymbiotic origin called the apicoplast. The P. falciparum apicoplast contains a 35 kb, circular DNA genome with limited coding capacity that lacks genes encoding proteins for DNA organization and replication. We report identification of a nuclear-encoded bacterial histone-like protein (PfHU) involved in DNA compaction in the apicoplast. PfHU is associated with apicoplast DNA and is expressed throughout the parasite's intra-erythocytic cycle. The protein binds DNA in a sequence nonspecific manner with a minimum binding site length of approximately 27 bp and a K(d) of approximately 63 nM and displays a preference for supercoiled DNA. PfHU is capable of condensing Escherichia coli nucleoids in vivo indicating its role in DNA compaction. The unique 42 aa C-terminal extension of PfHU influences its DNA condensation properties. In contrast to bacterial HUs that bend DNA, PfHU promotes concatenation of linear DNA and inhibits DNA circularization. Atomic Force Microscopic study of PfHU-DNA complexes shows protein concentration-dependent DNA stiffening, intermolecular bundling and formation of DNA bridges followed by assembly of condensed DNA networks. Our results provide the first functional characterization of an apicomplexan HU protein and provide additional evidence for red algal ancestry of the apicoplast.

Indexed as

Amino Acid SequenceAnimalsDNA-Binding ProteinsDNA, ConcatenatedDNA, ProtozoanMicroscopy, Atomic ForceModels, MolecularMolecular Sequence DataPlasmodium falciparumPlastidsProtein FoldingProtozoan ProteinsSequence Homology, Amino AcidDNA-Binding ProteinsDNA, ConcatenatedDNA, ProtozoanProtozoan Proteins

Identifiers

PMID18663012
PMCPMC2528193
OpenAlexW2170442112

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.