Evidence map›Paper›PMID 19344532›Full record

ArticleBMC plant biology2009

Plastid chaperonin proteins Cpn60 alpha and Cpn60 beta are required for plastid division in Arabidopsis thaliana.

Kenji Suzuki, Hiromitsu Nakanishi, Joyce Bower, David W Yoder, Katherine W Osteryoung, Shin-ya Miyagishima

Open access · goldAbstract read
In one paragraph

Article in BMC plant biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

46 citing papers in PubMed, 105 citations in OpenAlex.

  1. Review
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  5. Elevated Temperature Effects on Protein Turnover Dynamics inInternational journal of molecular sciences · 2024
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  11. Proceedings of the National Academy of Sciences of the United States of America · 2022
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  14. Review
  15. Article
  16. OsCpn60β1 is Essential for Chloroplast Development in Rice (International journal of molecular sciences · 2020
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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

6 authors at 2 institutions in 2 countries.

Kenji SuzukiInitiative Research Program, Advanced Science Institute, RIKEN, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan. kenkensuzuki@riken.jp
Hiromitsu Nakanishi
Joyce Bower
David W Yoder
Katherine W Osteryoung
Shin-ya Miyagishima
Michigan State University · USRIKEN Advanced Science Institute · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundPlastids arose from a free-living cyanobacterial endosymbiont and multiply by binary division as do cyanobacteria. Plastid division involves nucleus-encoded homologs of cyanobacterial division proteins such as FtsZ, MinD, MinE, and ARC6. However, homologs of many other cyanobacterial division genes are missing in plant genomes and proteins of host eukaryotic origin, such as a dynamin-related protein, PDV1 and PDV2 are involved in the division process. Recent identification of plastid division proteins has started to elucidate the similarities and differences between plastid division and cyanobacterial cell division. To further identify new proteins that are required for plastid division, we characterized previously and newly isolated plastid division mutants of Arabidopsis thaliana.

resultsLeaf cells of two mutants, br04 and arc2, contain fewer, larger chloroplasts than those of wild type. We found that ARC2 and BR04 are identical to nuclear genes encoding the plastid chaperonin 60 alpha (ptCpn60alpha) and chaperonin 60 beta (ptCpn60beta) proteins, respectively. In both mutants, plastid division FtsZ ring formation was partially perturbed though the level of FtsZ2-1 protein in plastids of ptcpn60beta mutants was similar to that in wild type. Phylogenetic analyses showed that both ptCpn60 proteins are derived from ancestral cyanobacterial proteins. The A. thaliana genome encodes two members of ptCpn60alpha family and four members of ptCpn60beta family respectively. We found that a null mutation in ptCpn60alpha abolished greening of plastids and resulted in an albino phenotype while a weaker mutation impairs plastid division and reduced chlorophyll levels. The functions of at least two ptCpn60beta proteins are redundant and the appearance of chloroplast division defects is dependent on the number of mutant alleles.

conclusionOur results suggest that both ptCpn60alpha and ptCpn60beta are required for the formation of a normal plastid division apparatus, as the prokaryotic counterparts are required for assembly of the cell division apparatus. Since moderate reduction of ptCpn60 levels impaired normal FtsZ ring formation but not import of FtsZ into plastids, it is suggested that the proper levels of ptCpn60 are required for folding of stromal plastid division proteins and/or regulation of FtsZ polymer dynamics.

Indexed as

ArabidopsisArabidopsis ProteinsChaperonin 60ChloroplastsCloning, MolecularDNA, PlantGene Expression Regulation, PlantGenes, PlantGenome, PlantMutagenesis, InsertionalMutationPhylogenyPlant LeavesPlant ProteinsPlants, Genetically ModifiedSequence AlignmentArabidopsis ProteinsChaperonin 60DNA, PlantFTSZ protein, ArabidopsisPlant Proteins

Identifiers

PMID19344532
PMCPMC2670834
OpenAlexW2017839625

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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.