Evidence map›Paper›PMID 30477420›Full record

ArticleBMC plant biology2018

Characterization of Dehydrin protein, CdDHN4-L and CdDHN4-S, and their differential protective roles against abiotic stress in vitro.

Aimin Lv, Liantai Su, Xingchen Liu, Qiang Xing, Bingru Huang, Yuan An, Peng Zhou

Abstract read
In one paragraph

Article in BMC plant biology, 2018. 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
–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

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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.

  1. Review
  2. Article
  3. Research Progress and Prospects of Molecular Breeding in Bermudagrass (International journal of molecular sciences · 2024
    Review
  4. Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Cellular Chaperone Function of Intrinsically Disordered Dehydrin ERD14.International journal of molecular sciences · 2021
    Article
  13. Article
  14. Article
  15. Article
  16. 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

7 authors.

Aimin LvSchool of Agriculture and Biology, Shanghai Jiao Tong University, Shanghai, 200240, People's Republic of China.
Liantai SuSchool of Agriculture and Biology, Shanghai Jiao Tong University, Shanghai, 200240, People's Republic of China.
Xingchen LiuSchool of Agriculture and Biology, Shanghai Jiao Tong University, Shanghai, 200240, People's Republic of China.
Qiang XingShanghai Chenshan Botanical Garden, Shanghai, 201602, People's Republic of China.
Bingru HuangDepartment of Plant Biology and Pathology, Rutgers, the State University of New Jersey, New Jersey, NJ, 08901, USA.
Yuan AnSchool of Agriculture and Biology, Shanghai Jiao Tong University, Shanghai, 200240, People's Republic of China. anyuan@sjtu.edu.cn.
Peng ZhouSchool of Agriculture and Biology, Shanghai Jiao Tong University, Shanghai, 200240, People's Republic of China. pzhou0063@sjtu.edu.cn.

Funding

Chinese Natural Science Foundation General Projects 31572451Chinese Natural Science Foundation General Projects 31872419National Key R&D Program of China 2017FY100600
6 · The paper itself

Abstract

backgroundDehydrins play positive roles in regulating plant abiotic stress responses. The objective of this study was to characterize two dehydrin genes, CdDHN4-L and CdDHN4-S, generated by alternative splicing of CdDHN4 in bermudagrass.

resultsOverexpression of CdDHN4-L with φ-segment and CdDHN4-S lacking of φ-segment in Arabidopsis significantly increased tolerance against abiotic stresses. The growth phenotype of Arabidopsis exposed to NaCl at 100 mM was better in plants overexpressing CdDHN4-L than those overexpressing CdDHN4-S, as well as better in E.coli cells overexpressing CdDHN4-L than those overexpressing CdDHN4-S in 300 and 400 mM NaCl, and under extreme temperature conditions at - 20 °C and 50 °C. The CdDHN4-L had higher disordered characterization on structures than CdDHN4-S at temperatures from 10 to 90 °C. The recovery activities of lactic dehydrogenase (LDH) and alcohol dehydrogenase (ADH) in presence of CdDHN4-L and CdDHN4-S were higher than that of LDH and ADH alone under freeze-thaw damage and heat. Protein-binding and bimolecular fluorescence complementation showed that both proteins could bind to proteins with positive isoelectric point via electrostatic forces.

conclusionsThese results indicate that CdDHN4-L has higher protective ability against abiotic stresses due to its higher flexible unfolded structure and thermostability in comparison with CdDHN4-S. These provided direct evidence of the function of the φ-segment in dehydrins for protecting plants against abiotic stress and to show the electrostatic interaction between dehydrins and client proteins.

Indexed as

Stress, PhysiologicalArabidopsisCloning, MolecularCynodonPlant ProteinsProtein BindingProtein Structure, SecondaryTemperaturedehydrin proteins, plantPlant ProteinsAbiotic stressDehydrinIntrinsic disorder proteinMolecular chaperoneProtein interactionφ-Segment

Identifiers

PMID30477420
PMCPMC6258397

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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.