Evidence map›Paper›PMID 23690600›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Structural insights into the N-terminal GIY-YIG endonuclease activity of Arabidopsis glutaredoxin AtGRXS16 in chloroplasts.

Xi Liu, Shian Liu, Yingang Feng, Jian-Zhong Liu, Yuling Chen, Khanh Pham, Haiteng Deng, Kendal D Hirschi, Xinquan Wang, Ninghui Cheng

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
0.9field-weighted citation impact, top 25% 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

18 citing papers in PubMed, 41 citations in OpenAlex.

  1. Emerging roles of glutaredoxins in plant metabolism.Journal of experimental botany · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. Identification and Function of Apicoplast Glutaredoxins inInternational journal of molecular sciences · 2021
    Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Mining for protein S-sulfenylation inProceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Protein networks identify novel symbiogenetic genes resulting from plastid endosymbiosis.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  17. Article
  18. 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

10 authors at 5 institutions in 2 countries.

Xi LiuMinistry of Education Key Laboratory of Protein Science, Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing 100084, China.
Shian Liu
Yingang Feng
Jian-Zhong Liu
Yuling Chen
Khanh Pham
Haiteng Deng
Kendal D Hirschi
Xinquan Wang
Ninghui Cheng
Tsinghua University · CNChildren's Nutrition Research Center at Baylor College of Medicine · USBaylor College of Medicine · USQingdao Institute of Bioenergy and Bioprocess Technology · CNZhejiang Normal University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glutaredoxins (Grxs) have been identified across taxa as important mediators in various physiological functions. A chloroplastic monothiol glutaredoxin, AtGRXS16 from Arabidopsis thaliana, comprises two distinct functional domains, an N-terminal domain (NTD) with GlyIleTyr-TyrIleGly (GIY-YIG) endonuclease motif and a C-terminal Grx module, to coordinate redox regulation and DNA cleavage in chloroplasts. Structural determination of AtGRXS16-NTD showed that it possesses a GIY-YIG endonuclease fold, but the critical residues for the nuclease activity are different from typical GIY-YIG endonucleases. AtGRXS16-NTD was able to cleave λDNA and chloroplast genomic DNA, and the nuclease activity was significantly reduced in AtGRXS16. Functional analysis indicated that AtGRXS16-NTD could inhibit the ability of AtGRXS16 to suppress the sensitivity of yeast grx5 cells to oxidative stress; however, the C-terminal Grx domain itself and AtGRXS16 with a Cys123Ser mutation were active in these cells and able to functionally complement a Grx5 deficiency in yeast. Furthermore, the two functional domains were shown to be negatively regulated through the formation of an intramolecular disulfide bond. These findings unravel a manner of regulation for Grxs and provide insights into the mechanistic link between redox regulation and DNA metabolism in chloroplasts.

Indexed as

Amino Acid MotifsAntiportersArabidopsisArabidopsis ProteinsCarrier ProteinsChloroplastsChromatography, GelDNAEndonucleasesGlutaredoxinsMagnetic Resonance SpectroscopyMass SpectrometryMutation, MissenseOxidation-ReductionProtein FoldingProtein Structure, TertiaryAntiportersArabidopsis ProteinsCarrier ProteinsCXIP1 protein, ArabidopsisDNAEndonucleasesGlutaredoxinsGrx5 protein, S cerevisiaeGRXS16 protein, ArabidopsisReactive Oxygen SpeciesSaccharomyces cerevisiae Proteinsnuclear magnetic resonancereactive oxygen species

Identifiers

PMID23690600
PMCPMC3677505
OpenAlexW2110691019

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.