Evidence map›Paper›PMID 25228689›Full record

ArticleThe Journal of biological chemistry2014

A thylakoid membrane protein harboring a DnaJ-type zinc finger domain is required for photosystem I accumulation in plants.

Rikard Fristedt, Rosalind Williams-Carrier, Sabeeha S Merchant, Alice Barkan

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

44 citing papers in PubMed, 68 citations in OpenAlex.

  1. Article
  2. Review
  3. On the non-oxygenic origins of thylakoids.Communications biology · 2025
    Review
  4. Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. The maize callose synthaseMolecular breeding : new strategies in plant improvement · 2023
    Article
  17. Article
  18. Review
  19. Article
  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

4 authors at 2 institutions in 1 country.

Rikard FristedtDepartment of Chemistry and Biochemistry and UCLA, Los Angeles, California 90095; Institute for Genomics and Proteomics, UCLA, Los Angeles, California 90095 and.
Rosalind Williams-CarrierInstitute of Molecular Biology, University of Oregon, Eugene, Oregon 97403.
Sabeeha S MerchantDepartment of Chemistry and Biochemistry and UCLA, Los Angeles, California 90095; Institute for Genomics and Proteomics, UCLA, Los Angeles, California 90095 and.
Alice BarkanInstitute of Molecular Biology, University of Oregon, Eugene, Oregon 97403. Electronic address: abarkan@uoregon.edu.
University of California, Los Angeles · USUniversity of Oregon · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Photosystem I (PSI) is a large pigment-protein complex and one of the two photosystems that drive electron transfer in oxygenic photosynthesis. We identified a nuclear gene required specifically for the accumulation of PSI in a forward genetic analysis of chloroplast biogenesis in maize. This gene, designated psa2, belongs to the "GreenCut" gene set, a group of genes found in green algae and plants but not in non-photosynthetic organisms. Disruption of the psa2 ortholog in Arabidopsis likewise resulted in the specific loss of PSI proteins. PSA2 harbors a conserved domain found in DnaJ chaperones where it has been shown to form a zinc finger and to have protein-disulfide isomerase activity. Accordingly, PSA2 exhibited protein-disulfide reductase activity in vitro. PSA2 localized to the thylakoid lumen and was found in a ∼250-kDa complex harboring the peripheral PSI protein PsaG but lacking several core PSI subunits. PSA2 mRNA is coexpressed with mRNAs encoding various proteins involved in the biogenesis of the photosynthetic apparatus with peak expression preceding that of genes encoding structural components. PSA2 protein abundance was not decreased in the absence of PSI but was reduced in the absence of the PSI assembly factor Ycf3. These findings suggest that a complex harboring PSA2 and PsaG mediates thiol transactions in the thylakoid lumen that are important for the assembly of PSI.

Indexed as

Amino Acid SequenceArabidopsisArabidopsis ProteinsBase SequenceChlorophyllCystineGene Knockout TechniquesKineticsMolecular Sequence DataOxidation-ReductionPhotosynthesisPhotosystem I Protein ComplexPlant LeavesProtein Interaction MappingProtein TransportSequence DeletionArabidopsis ProteinsChlorophyllCystinePhotosystem I Protein ComplexPsa2 protein, ArabidopsisArabidopsisChaperone DnaJ (DnaJ)ChloroplastMaizeMembrane BiogenesisPhotosynthesisProtein-disulfide IsomeraseThylakoid Lumen

Identifiers

PMID25228689
PMCPMC4215244
OpenAlexW2061434909

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.