Evidence map›Paper›PMID 12119376›Full record

ArticleThe Plant cell2002

Detection and localization of a chloroplast-encoded HU-like protein that organizes chloroplast nucleoids.

Tamaki Kobayashi, Manabu Takahara, Shin-ya Miyagishima, Haruko Kuroiwa, Narie Sasaki, Niji Ohta, Motomichi Matsuzaki, Tsuneyoshi Kuroiwa

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The Plant cell, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

30 citing papers in PubMed, 84 citations in OpenAlex.

  1. Article
  2. Article
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  4. 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
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  12. Review
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  15. Eukaryotic-type plastid nucleoid protein pTAC3 is essential for transcription by the bacterial-type plastid RNA polymerase.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  16. Article
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  19. Mechanisms of organelle division and inheritance and their implications regarding the origin of eukaryotic cells.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2010
    Review
  20. 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

8 authors at 3 institutions in 1 country.

Tamaki KobayashiDepartment of Biological Science, Graduate School of Science, University of Tokyo, Tokyo 113-0033, Japan. tamaki@biol.s.u-tokyo.ac.jp
Manabu Takahara
Shin-ya Miyagishima
Haruko Kuroiwa
Narie Sasaki
Niji Ohta
Motomichi Matsuzaki
Tsuneyoshi Kuroiwa
Tokyo University of Science · JPOchanomizu University · JPSaitama University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Chloroplast DNA (cpDNA) is packed into discrete structures called chloroplast nucleoids (cp-nucleoids). The structure of cpDNA is thought to be important for its maintenance and regulation. In bacteria and mitochondria, histone-like proteins (such as HU and Abf2, respectively) are abundant and play important roles in DNA organization. However, a primary structural protein has yet to be found in cp-nucleoids. Here, we identified an abundant DNA binding protein from isolated cp-nucleoids of the primitive red alga Cyanidioschyzon merolae. The purified protein had sequence homology with the bacterial histone-like protein HU, and it complemented HU-lacking Escherichia coli mutants. The protein, called HC (histone-like protein of chloroplast), was encoded by a single gene (CmhupA) in the C. merolae chloroplast genome. Using immunofluorescence and immunoelectron microscopy, we demonstrated that HC was distributed uniformly throughout the entire cp-nucleoid. The protein was expressed constitutively throughout the cell and the chloroplast division cycle, and it was able to condense DNA. These results indicate that HC, a bacteria-derived histone-like protein, primarily organizes cpDNA into the nucleoid.

Indexed as

Saccharomyces cerevisiae ProteinsAlgal ProteinsAmino Acid SequenceBacterial ProteinsChloroplastsDNA-Binding ProteinsDNA, ChloroplastEscherichia coliGenetic Complementation TestImmunoblottingMolecular Sequence DataMutationRhodophytaSequence Homology, Amino AcidTranscription FactorsABF2 protein, S cerevisiaeAlgal ProteinsBacterial ProteinsDNA-Binding ProteinsDNA, Chloroplasthistone-like protein HU, bacteriaSaccharomyces cerevisiae ProteinsTranscription Factors

Identifiers

PMID12119376
PMCPMC150708
OpenAlexW2166869374

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.