iTRAQ-based proteomic analysis provides insights into the molecular mechanisms of rice formyl tetrahydrofolate deformylase in salt response.


Journal

Planta
ISSN: 1432-2048
Titre abrégé: Planta
Pays: Germany
ID NLM: 1250576

Informations de publication

Date de publication:
17 Sep 2021
Historique:
received: 10 04 2021
accepted: 05 09 2021
entrez: 17 9 2021
pubmed: 18 9 2021
medline: 22 9 2021
Statut: epublish

Résumé

A new molecular mechanism of tetrahydrofolate deformylase involved in the salt response presumably affects mitochondrial and chloroplast function by regulating energy metabolism and accumulation of reactive oxygen species. High salinity severely restrains plant growth and development, consequently leading to a reduction in grain yield. It is therefore critical to identify the components involved in plant salt resistance. In our previous study, we identified a rice leaf early-senescence mutant hpa1, which encodes a formyl tetrahydrofolate deformylase (Xiong et al. in Sci China Life Sci 64(5):720-738, 2021). Here, we report that HPA1 also plays a role in the salt response. To explore the molecular mechanism of HPA1 in salt resistance, we attempted to identify the differentially expressed proteins between wild type and hpa1 mutant for salinity treatment using an iTRAQ-based comparative protein quantification approach. A total of 4598 proteins were identified, of which 279 were significantly altered, including 177 up- and 102 down-regulated proteins. A functional analysis suggested that the 279 differentially expressed proteins are involved mainly in the regulation of oxidative phosphorylation, phenylpropanoid biosynthesis, photosynthesis, posttranslational modifications, protein turnover and energy metabolism. Moreover, a deficiency in HPA1 impaired chlorophyll metabolism and photosynthesis in chloroplasts and affected the electron flow of the electron transport chain in mitochondria. These changes led to abnormal energy metabolism and accumulation of reactive oxygen species, which may affect the permeability and integrity of cell membranes, leading to cell death. In addition, the results were verified by transcriptional or physiological experiments. Our results provide an insight into a new molecular mechanism of the tetrahydrofolate cycle protein formyl tetrahydrofolate deformylase, which is involved in the salt response, presumably by affecting mitochondrial and chloroplast function regulating energy metabolism and accumulation of reactive oxygen species under salt stress.

Identifiants

pubmed: 34533642
doi: 10.1007/s00425-021-03723-z
pii: 10.1007/s00425-021-03723-z
doi:

Substances chimiques

Plant Proteins 0
Tetrahydrofolates 0

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

76

Subventions

Organisme : the National Key Research and Development Program of China
ID : 2016YFD0101801
Organisme : the National Natural Science Foundation of China
ID : 91735303
Organisme : the National Natural Science Foundation of China
ID : 91335103
Organisme : the Natural Science Foundation of Zhejiang
ID : LY18C130010
Organisme : the Natural Science Foundation of Zhejiang
ID : LY18C130009
Organisme : the Natural Science Foundation of Zhejiang
ID : LY20C130004
Organisme : the Science and Technology Project of Hangzhou
ID : 20180432B03
Organisme : the Science and Technology Project of Hangzhou
ID : 20180432B09
Organisme : the Science and Technology Project of Hangzhou
ID : 20180432B04
Organisme : the foundation of Zhejiang education department
ID : Y201431296
Organisme : the natural science foundation zhejiang
ID : LGN19C130006

Informations de copyright

© 2021. The Author(s), under exclusive licence to Springer-Verlag GmbH Germany, part of Springer Nature.

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Auteurs

Erhui Xiong (E)

College of Life and Environmental Sciences, Hangzhou Normal University, Hangzhou, 311121, China.

Chen Zhang (C)

College of Life and Environmental Sciences, Hangzhou Normal University, Hangzhou, 311121, China.

Chenxi Ye (C)

College of Life and Environmental Sciences, Hangzhou Normal University, Hangzhou, 311121, China.

Yaohuang Jiang (Y)

College of Life and Environmental Sciences, Hangzhou Normal University, Hangzhou, 311121, China.

Yanli Zhang (Y)

College of Life and Environmental Sciences, Hangzhou Normal University, Hangzhou, 311121, China.

Fei Chen (F)

College of Life and Environmental Sciences, Hangzhou Normal University, Hangzhou, 311121, China.

Guojun Dong (G)

State Key Laboratory for Rice Biology, China National Rice Research Institute, Hangzhou, 310006, Zhejiang, China.

Dali Zeng (D)

State Key Laboratory for Rice Biology, China National Rice Research Institute, Hangzhou, 310006, Zhejiang, China.

Yanchun Yu (Y)

College of Life and Environmental Sciences, Hangzhou Normal University, Hangzhou, 311121, China. ycyu@hznu.edu.cn.

Limin Wu (L)

College of Life and Environmental Sciences, Hangzhou Normal University, Hangzhou, 311121, China. lmwu2011@hznu.edu.cn.

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