Evidence map›Paper›PMID 12642673›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2003

ARC5, a cytosolic dynamin-like protein from plants, is part of the chloroplast division machinery.

Hongbo Gao, Deena Kadirjan-Kalbach, John E Froehlich, Katherine W Osteryoung

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 122 papers.

0numbers the graph read from it
0cells of the map it votes in
122citing papers in PubMed
6.8field-weighted citation impact, top 2% 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

122 citing papers in PubMed, 291 citations in OpenAlex.

  1. Article
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  4. A multiplant transcriptomic atlas reveals conserved and lineage-specific defense architectures in response toProceedings of the National Academy of Sciences of the United States of America · 2026
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  8. The dynamin-related proteinFrontiers in plant science · 2026
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  10. Genomes of nitrogen-fixing eukaryotes reveal an alternate path for organellogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  11. Antiviral Mx proteins have an ancient origin and widespread distribution among eukaryotes.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
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62 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Hongbo GaoDepartment of Plant Biology, 166 Plant Biology Building, Michigan State University, East Lansing, MI 48824, USA.
Deena Kadirjan-Kalbach
John E Froehlich
Katherine W Osteryoung
Michigan State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Chloroplast division in plant cells is orchestrated by a complex macromolecular machine with components positioned on both the inner and outer envelope surfaces. The only plastid division proteins identified to date are of endosymbiotic origin and are localized inside the organelle. Employing positional cloning methods in Arabidopsis in conjunction with a novel strategy for pinpointing the mutant locus, we have identified a gene encoding a new chloroplast division protein, ARC5. Mutants of ARC5 exhibit defects in chloroplast constriction, have enlarged, dumbbell-shaped chloroplasts, and are rescued by a wild-type copy of ARC5. The ARC5 gene product shares similarity with the dynamin family of GTPases, which mediate endocytosis, mitochondrial division, and other organellar fission and fusion events in eukaryotes. Phylogenetic analysis showed that ARC5 is related to a group of dynamin-like proteins unique to plants. A GFP-ARC5 fusion protein localizes to a ring at the chloroplast division site. Chloroplast import and protease protection assays indicate that the ARC5 ring is positioned on the outer surface of the chloroplast. Thus, ARC5 is the first cytosolic component of the chloroplast division complex to be identified. ARC5 has no obvious counterparts in prokaryotes, suggesting that it evolved from a dynamin-related protein present in the eukaryotic ancestor of plants. These results indicate that the chloroplast division apparatus is of mixed evolutionary origin and that it shares structural and mechanistic similarities with both the cell division machinery of bacteria and the dynamin-mediated organellar fission machineries of eukaryotes.

Indexed as

Amino Acid SequenceArabidopsisArabidopsis ProteinsChloroplastsCloning, MolecularDNA PrimersDynaminsLuciferasesMolecular Sequence DataPlants, Genetically ModifiedPolymerase Chain ReactionSequence AlignmentSequence Homology, Amino AcidArabidopsis ProteinsARC5 protein, ArabidopsisDNA PrimersDynaminsLuciferases

Identifiers

PMID12642673
PMCPMC153092
OpenAlexW1968827563

What OpenQuestion holds

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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.