Maize Sep15‐like functions in endoplasmic reticulum and reactive oxygen species homeostasis to promote salt and osmotic stress resistance. (4th February 2019)
- Record Type:
- Journal Article
- Title:
- Maize Sep15‐like functions in endoplasmic reticulum and reactive oxygen species homeostasis to promote salt and osmotic stress resistance. (4th February 2019)
- Main Title:
- Maize Sep15‐like functions in endoplasmic reticulum and reactive oxygen species homeostasis to promote salt and osmotic stress resistance
- Authors:
- Zhu, Jiantang
Wang, Guangling
Li, Cuiling
Li, Qingqing
Gao, Yankun
Chen, Fanguo
Xia, Guangmin - Abstract:
- Abstract: In animals, the Sep15 protein participates in disease resistance, growth, and development, but the function of its plant homologues remains unclear. Here, the function of maize Sep15 was analysed by characterization of two independent Sep15‐like loss‐of‐function mutants. In the absence of ZmSep15‐like, seedling tolerance to both water and salinity stress was compromised. The mutants experienced a heightened level of endoplasmic reticulum stress, and over‐accumulated reactive oxygen species, resulting in leaf necrosis. Characterization of Arabidopsis thaliana atsep15 mutant as well as like with ectopic expression of ZmSep15‐like indicated that ZmSep15‐like contributed to tolerance of both osmotic and salinity stress. ZmSep15‐like interacted physically with UDP‐glucose: glycoprotein glucosyltransferase1 (UGGT1). When the interaction was disrupted, the response to both osmotic and salinity stresses was impaired in maize or Arabidopsis. Co‐expressing ZmUGGT1 and ZmUGGT2 enhanced the tolerance of A . thaliana to both stressors, indicating a functional interaction between them. Together, the data indicated that plants Sep15‐like proteins promote osmotic and salinity stress resistance by influencing endoplasmic reticulum stress response and reactive oxygen species level. Abstract : Although the molecular basis and function of certain members of the Sep15 protein have been defined in animals, the function of its plant homologues remains unclear. Here, a functionalAbstract: In animals, the Sep15 protein participates in disease resistance, growth, and development, but the function of its plant homologues remains unclear. Here, the function of maize Sep15 was analysed by characterization of two independent Sep15‐like loss‐of‐function mutants. In the absence of ZmSep15‐like, seedling tolerance to both water and salinity stress was compromised. The mutants experienced a heightened level of endoplasmic reticulum stress, and over‐accumulated reactive oxygen species, resulting in leaf necrosis. Characterization of Arabidopsis thaliana atsep15 mutant as well as like with ectopic expression of ZmSep15‐like indicated that ZmSep15‐like contributed to tolerance of both osmotic and salinity stress. ZmSep15‐like interacted physically with UDP‐glucose: glycoprotein glucosyltransferase1 (UGGT1). When the interaction was disrupted, the response to both osmotic and salinity stresses was impaired in maize or Arabidopsis. Co‐expressing ZmUGGT1 and ZmUGGT2 enhanced the tolerance of A . thaliana to both stressors, indicating a functional interaction between them. Together, the data indicated that plants Sep15‐like proteins promote osmotic and salinity stress resistance by influencing endoplasmic reticulum stress response and reactive oxygen species level. Abstract : Although the molecular basis and function of certain members of the Sep15 protein have been defined in animals, the function of its plant homologues remains unclear. Here, a functional characterization of a maize Sep15 homologue has been presented: ZmSep15‐like, interacting with UDP‐glucose: glycoprotein glucosyltransferase1 (UGGT1), made a contribution to the tolerance of both osmotic and salinity stress by involving in ER stress. … (more)
- Is Part Of:
- Plant, cell and environment. Volume 42:Number 5(2019)
- Journal:
- Plant, cell and environment
- Issue:
- Volume 42:Number 5(2019)
- Issue Display:
- Volume 42, Issue 5 (2019)
- Year:
- 2019
- Volume:
- 42
- Issue:
- 5
- Issue Sort Value:
- 2019-0042-0005-0000
- Page Start:
- 1486
- Page End:
- 1502
- Publication Date:
- 2019-02-04
- Subjects:
- cell death -- endoplasmic reticulum stress -- redox homeostasis -- UDP‐glucose: Glycoprotein glucosyltransferase -- Zea mays mutant -- ZmSep15‐like
Plant physiology -- Periodicals
Plant cells and tissues -- Periodicals
Plant communities -- Periodicals
581.105 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1365-3040 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1111/pce.13507 ↗
- Languages:
- English
- ISSNs:
- 0140-7791
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 6514.200000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 9829.xml