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A calmodulin-like protein PvCML9 negatively regulates salt tolerance.

Authors :
Yang M
Zhou B
Song Z
Tan Z
Liu R
Luo Y
Guo Z
Lu S
Source :
Plant physiology and biochemistry : PPB [Plant Physiol Biochem] 2024 May; Vol. 210, pp. 108642. Date of Electronic Publication: 2024 Apr 18.
Publication Year :
2024

Abstract

Calmodulin-like proteins (CMLs) are unique Ca <superscript>2+</superscript> sensors and play crucial roles in response to abiotic stress in plants. A salt-repressed PvCML9 from halophyte seashore paspalum (Paspalum vaginatum O. Swartz) was identified. PvCML9 was localized in the cytoplasm and nucleus and highly expressed in roots and stems. Overexpression of PvCML9 led to reduced salt tolerance in rice and seashore paspalum, whereas downregulating expression of PvCML9 showed increased salt tolerance in seashore paspalum as compared with the wild type (WT), indicating that PvCML9 regulated salt tolerance negatively. Na <superscript>+</superscript> and K <superscript>+</superscript> homeostasis was altered by PvCML9 expression. Lower level of Na <superscript>+</superscript> /K <superscript>+</superscript> ratio in roots and shoots was maintained in PvCML9-RNAi lines compared with WT under salt stress, but higher level in overexpression lines. Moreover, higher levels of SOD and CAT activities and proline accumulation were observed in PvCML9-RNAi lines compared with WT under salt stress, but lower levels in overexpression lines, which altered ROS homeostasis. Based on the above data, mutation of its homolog gene OsCML9 in rice by CRISPR/Cas9 was performed. The mutant had enhanced salt tolerance without affecting rice growth and development, suggesting that OsCML9 gene is an ideal target gene to generate salt tolerant cultivars by genome editing in the future.<br />Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.<br /> (Copyright © 2024. Published by Elsevier Masson SAS.)

Details

Language :
English
ISSN :
1873-2690
Volume :
210
Database :
MEDLINE
Journal :
Plant physiology and biochemistry : PPB
Publication Type :
Academic Journal
Accession number :
38643538
Full Text :
https://doi.org/10.1016/j.plaphy.2024.108642