Overexpression of calmodulin gene fragment from Antarctic notothenioid fish improves chilling tolerance in Nicotiana benthamiana

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...

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Bibliographic Details
Published in:Photosynthetica
Main Authors: Zhang, T. J., Pan, L. J., Huang, Qingrong, Zhu, L. H., Yang, N., Peng, C. L., Chen, L. B.
Language:English
Subjects:
obecná botanika
general botany
calcium-binding protein
chilling stress
chlorophyll fluorescence
electrolyte leakage
2
581
Antarctic
Antarc*
Online Access:https://kramerius.lib.cas.cz/view/uuid:0cbb9a33-70ee-4e5a-986a-cf1eec1f15ae
https://doi.org/10.1007/s11099-016-0682-z
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Summary: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 4◦C or 0◦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. T. J. Zhang, L. J. Pan, Q. Huang, L. H. Zhu, N. Yang, C. L. Peng, L. B. Chen. Obsahuje seznam literatury

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