Evidence map›Paper›PMID 26912459›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

ATP binding by the P-loop NTPase OsYchF1 (an unconventional G protein) contributes to biotic but not abiotic stress responses.

Ming-Yan Cheung, Xiaorong Li, Rui Miao, Yu-Hang Fong, Kwan-Pok Li, Yuk-Lin Yung, Mei-Hui Yu, Kam-Bo Wong, Zhongzhou Chen, Hon-Ming Lam

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
–field-weighted citation impact
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

26 citing papers in PubMed.

  1. Article
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  9. Review
  10. Review
  11. AtGAP1 Promotes the Resistance toInternational journal of molecular sciences · 2022
    Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. DistinctiveFrontiers in plant science · 2022
    Article
  17. Review
  18. Article
  19. Article
  20. UMP Kinase Regulates Chloroplast Development and Cold Response in Rice.International journal of molecular sciences · 2019
    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.

Ming-Yan CheungSchool of Life Sciences, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong SAR; Center for Soybean Research of the State Key Laboratory of Agrobiotechnology, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong SAR;
Xiaorong LiState Key Laboratory of Agrobiotechnology, China Agricultural University, Beijing 100193, China;
Rui MiaoSchool of Life Sciences, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong SAR; Center for Soybean Research of the State Key Laboratory of Agrobiotechnology, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong SAR;
Yu-Hang FongSchool of Life Sciences, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong SAR; Center for Protein Sciences and Crystallography, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong SAR.
Kwan-Pok LiSchool of Life Sciences, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong SAR; Center for Soybean Research of the State Key Laboratory of Agrobiotechnology, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong SAR;
Yuk-Lin YungSchool of Life Sciences, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong SAR; Center for Soybean Research of the State Key Laboratory of Agrobiotechnology, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong SAR;
Mei-Hui YuSchool of Life Sciences, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong SAR; Center for Soybean Research of the State Key Laboratory of Agrobiotechnology, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong SAR;
Kam-Bo WongSchool of Life Sciences, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong SAR; Center for Protein Sciences and Crystallography, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong SAR honming@cuhk.edu.hk kbwong@cuhk.edu.hk chenzhongzhou@cau.edu.cn.
Zhongzhou ChenState Key Laboratory of Agrobiotechnology, China Agricultural University, Beijing 100193, China; honming@cuhk.edu.hk kbwong@cuhk.edu.hk chenzhongzhou@cau.edu.cn.ORCID http://orcid.org/0000-0003-1319-9664
Hon-Ming LamSchool of Life Sciences, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong SAR; Center for Soybean Research of the State Key Laboratory of Agrobiotechnology, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong SAR; honming@cuhk.edu.hk kbwong@cuhk.edu.hk chenzhongzhou@cau.edu.cn.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

G proteins are involved in almost all aspects of the cellular regulatory pathways through their ability to bind and hydrolyze GTP. The YchF subfamily, interestingly, possesses the unique ability to bind both ATP and GTP, and is possibly an ancestral form of G proteins based on phylogenetic studies and is present in all kingdoms of life. However, the biological significance of such a relaxed ligand specificity has long eluded researchers. Here, we have elucidated the different conformational changes caused by the binding of a YchF homolog in rice (OsYchF1) to ATP versus GTP by X-ray crystallography. Furthermore, by comparing the 3D relationships of the ligand position and the various amino acid residues at the binding sites in the crystal structures of the apo-bound and ligand-bound versions, a mechanism for the protein's ability to bind both ligands is revealed. Mutation of the noncanonical G4 motif of the OsYchF1 to the canonical sequence for GTP specificity precludes the binding/hydrolysis of ATP and prevents OsYchF1 from functioning as a negative regulator of plant-defense responses, while retaining its ability to bind/hydrolyze GTP and its function as a negative regulator of abiotic stress responses, demonstrating the specific role of ATP-binding/hydrolysis in disease resistance. This discovery will have a significant impact on our understanding of the structure-function relationships of the YchF subfamily of G proteins in all kingdoms of life.

Indexed as

Protein Structure, SecondaryProtein Structure, TertiaryAdenosine TriphosphateAmino Acid SequenceArabidopsisCrystallography, X-RayGene Expression Regulation, PlantGTP-Binding ProteinsHost-Pathogen InteractionsHydrogen-Ion ConcentrationModels, MolecularMolecular Sequence DataNucleoside-TriphosphataseOryzaPlant ProteinsPlants, Genetically ModifiedAdenosine TriphosphateGTP-Binding ProteinsNucleoside-TriphosphatasePlant ProteinsSodium ChlorideATP-binding proteinG proteinP-loop NTPaseX-ray crystallographyYchF

Identifiers

PMID26912459
PMCPMC4791026

What OpenQuestion holds

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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.