期刊
PHOTOSYNTHETICA
卷 55, 期 4, 页码 630-637出版社
ACAD SCIENCES CZECH REPUBLIC, INST EXPERIMENTAL BOTANY
DOI: 10.1007/s11099-016-0682-z
关键词
calcium-binding protein; chilling stress; chlorophyll fluorescence; electrolyte leakage; transgenic plants
资金
- 973 program from Ministry of Science and Technology of China [2010CB126304]
- National Natural Science Foundation of China [31570398, 31270287]
- International Collaborative Polar Exploration Grant from CHINARE
Calmodulin (CaM) is a highly conserved calcium sensor protein associated with chilling tolerance in living organisms. It has four EF-hand domains for binding of four Ca2+, two of them located in the N-terminus, and the other two in the C-terminus. A notothenioid CaM gene fragment (CaMm), which only codes for N-terminus of CaM (with two EF-hand domains), was introduced into Nicotiana benthamiana. Effects of its overexpression on chilling tolerance in plants were explored. During 4au broken vertical bar C or 0au broken vertical bar C chilling treatment, both CaMm and CaM transgenic plants showed higher PSII maximum quantum yield, actual quantum yield, and soluble protein content, lower electrolyte leakage and malondialdehyde content than that of the control. The changes in these physiological indices were comparable between the CaMm and CaM transgenic plants during the treatments. These results indicate that the N-terminus of calmodulin is likely the key functional domain involved in the adaptive response to cold stress.
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