umu.sePublications
Change search
Refine search result
1 - 1 of 1
CiteExportLink to result list
Permanent link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Rows per page
  • 5
  • 10
  • 20
  • 50
  • 100
  • 250
Sort
  • Standard (Relevance)
  • Author A-Ö
  • Author Ö-A
  • Title A-Ö
  • Title Ö-A
  • Publication type A-Ö
  • Publication type Ö-A
  • Issued (Oldest first)
  • Issued (Newest first)
  • Created (Oldest first)
  • Created (Newest first)
  • Last updated (Oldest first)
  • Last updated (Newest first)
  • Disputation date (earliest first)
  • Disputation date (latest first)
  • Standard (Relevance)
  • Author A-Ö
  • Author Ö-A
  • Title A-Ö
  • Title Ö-A
  • Publication type A-Ö
  • Publication type Ö-A
  • Issued (Oldest first)
  • Issued (Newest first)
  • Created (Oldest first)
  • Created (Newest first)
  • Last updated (Oldest first)
  • Last updated (Newest first)
  • Disputation date (earliest first)
  • Disputation date (latest first)
Select
The maximal number of hits you can export is 250. When you want to export more records please use the Create feeds function.
  • 1.
    Yang, Qi
    et al.
    Umeå University, Faculty of Science and Technology, Umeå Plant Science Centre (UPSC). Umeå University, Faculty of Science and Technology, Department of Plant Physiology. State Key Laboratory of Tree Genetics and Breeding, Chinese Academy of Forestry, Beijing, China.
    Liu, Yan-Jing
    Zeng, Qing-Yin
    Overexpression of three orthologous glutathione S-transferases from Populus increased salt and drought resistance in Arabidopsis2019In: Biochemical Systematics and Ecology, ISSN 0305-1978, E-ISSN 1873-2925, Vol. 83, p. 57-61Article in journal (Refereed)
    Abstract [en]

    Glutathione S-transferases (GSTs) are multifunctional proteins and play a role in detoxification of xenobiotics as well as prevention of oxidative damage. This study exogenously overexpressed PtGSTF4 from Populus trichocarpa and its two orthologs from Populus yatungensis and Populus euphratica in Arabidopsis thaliana, respectively. To elucidate the function of three GSTF4 proteins in stress response, we compared germination and seedling growth in transgenic Arabidopsis with salt and drought treatments. All three Populus GSTF4 genes overexpressed Arabidopsis showed enhanced resistance to salt stress and drought. GSTF4 transgenic plants accumulated less hydrogen peroxide and more chlorophylls and decreased levels of lipid peroxidation under salt stress and drought comparing to the mock control plants. The difference observed by GSH and GSSG measurements indicated GSTF4 proteins may involve in glutathione-dependent peroxide scavenging which lead to reduced oxidative damage. The Arabidopsis transformed with the GSTF4 gene form P. euphratica showed higher germination rate and different performance of affecting GSSG contents comparing with the other two orthologous GST genes under NaCl treatment. These results suggested three Populus GSTF4 orthologs may have functional divergence in stress responding. This study provides insights into molecular mechanisms that underlie salt and drought stress tolerance of Phi GSTs and gives evidence for the functional divergence among orthologs in vivo.

1 - 1 of 1
CiteExportLink to result list
Permanent link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf