Evidence map›Paper›PMID 27208269›Full record

ArticlePlant physiology2016

BIOGENESIS FACTOR REQUIRED FOR ATP SYNTHASE 3 Facilitates Assembly of the Chloroplast ATP Synthase Complex.

Lin Zhang, Zhikun Duan, Jiao Zhang, Lianwei Peng

Open access · bronzeAbstract read
In one paragraph

Article in Plant physiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.7field-weighted citation impact, top 15% 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

21 citing papers in PubMed, 33 citations in OpenAlex.

  1. Review
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  13. An Exon Skipping inInternational journal of molecular sciences · 2021
    Article
  14. Article
  15. Involvement of Lhcb6 and Lhcb5 in Photosynthesis Regulation inInternational journal of molecular sciences · 2019
    Article
  16. Article
  17. Article
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  20. Review
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 3 institutions in 1 country.

Lin ZhangKey Laboratory of Photobiology, CAS Center for Excellence in Molecular Plant Sciences, Institute of Botany, Chinese Academy of Sciences, Beijing 100093, China (L.Z., Z.D., J.Z., L.P.); andUniversity of Chinese Academy of Sciences, Beijing 100049, China (L.Z., Z.D.).
Zhikun DuanKey Laboratory of Photobiology, CAS Center for Excellence in Molecular Plant Sciences, Institute of Botany, Chinese Academy of Sciences, Beijing 100093, China (L.Z., Z.D., J.Z., L.P.); andUniversity of Chinese Academy of Sciences, Beijing 100049, China (L.Z., Z.D.).
Jiao ZhangKey Laboratory of Photobiology, CAS Center for Excellence in Molecular Plant Sciences, Institute of Botany, Chinese Academy of Sciences, Beijing 100093, China (L.Z., Z.D., J.Z., L.P.); andUniversity of Chinese Academy of Sciences, Beijing 100049, China (L.Z., Z.D.).
Lianwei PengKey Laboratory of Photobiology, CAS Center for Excellence in Molecular Plant Sciences, Institute of Botany, Chinese Academy of Sciences, Beijing 100093, China (L.Z., Z.D., J.Z., L.P.); andUniversity of Chinese Academy of Sciences, Beijing 100049, China (L.Z., Z.D.) penglianwei@ibcas.ac.cn.
Chinese Academy of Sciences · CNCenter for Excellence in Molecular Plant Sciences · CNInstitute of Botany · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Thylakoid membrane-localized chloroplast ATP synthases use the proton motive force generated by photosynthetic electron transport to produce ATP from ADP. Although it is well known that the chloroplast ATP synthase is composed of more than 20 proteins with α3β3γ1ε1δ1I1II1III14IV1 stoichiometry, its biogenesis process is currently unclear. To unravel the molecular mechanisms underlying the biogenesis of chloroplast ATP synthase, we performed extensive screening for isolating ATP synthase mutants in Arabidopsis (Arabidopsis thaliana). In the recently identified bfa3 (biogenesis factors required for ATP synthase 3) mutant, the levels of chloroplast ATP synthase subunits were reduced to approximately 25% of wild-type levels. In vivo labeling analysis showed that assembly of the CF1 component of chloroplast ATP synthase was less efficient in bfa3 than in the wild type, indicating that BFA3 is required for CF1 assembly. BFA3 encodes a chloroplast stromal protein that is conserved in higher plants, green algae, and a few species of other eukaryotic algae, and specifically interacts with the CF1β subunit. The BFA3 binding site was mapped to a region in the catalytic site of CF1β. Several residues highly conserved in eukaryotic CF1β are crucial for the BFA3-CF1β interaction, suggesting a coevolutionary relationship between BFA3 and CF1β. BFA3 appears to function as a molecular chaperone that transiently associates with unassembled CF1β at its catalytic site and facilitates subsequent association with CF1α during assembly of the CF1 subcomplex of chloroplast ATP synthase.

Indexed as

ArabidopsisArabidopsis ProteinsChloroplast Proton-Translocating ATPasesMembrane ProteinsMutationPhenotypePhotosynthesisProtein BindingProtein Interaction MappingProtein SubunitsThylakoidsArabidopsis Proteinsbiogenesis factor required for ATP synthase 3, ArabidopsisChloroplast Proton-Translocating ATPasesMembrane ProteinsProtein Subunits

Identifiers

PMID27208269
PMCPMC4902607
OpenAlexW2417561484

What OpenQuestion holds

Textmetadata
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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.