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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ftczechacademysc:oai:kramerius.lib.cas.cz:uuid:0cbb9a33-70ee-4e5a-986a-cf1eec1f15ae 2024-03-17T08:53:28+00:00 Overexpression of calmodulin gene fragment from Antarctic notothenioid fish improves chilling tolerance in Nicotiana benthamiana Zhang, T. J. Pan, L. J. Huang, Qingrong Zhu, L. H. Yang, N. Peng, C. L. Chen, L. B. 630-637 print média svazek https://kramerius.lib.cas.cz/view/uuid:0cbb9a33-70ee-4e5a-986a-cf1eec1f15ae https://doi.org/10.1007/s11099-016-0682-z eng eng https://kramerius.lib.cas.cz/view/uuid:0cbb9a33-70ee-4e5a-986a-cf1eec1f15ae issn:0300-3604 doi:10.1007/s11099-016-0682-z policy:public obecná botanika general botany calcium-binding protein chilling stress chlorophyll fluorescence electrolyte leakage 2 581 ftczechacademysc https://doi.org/10.1007/s11099-016-0682-z 2024-02-19T23:08:28Z 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 Other/Unknown Material Antarc* Antarctic Czech Academy of Sciences: dKNAV Antarctic Photosynthetica 55 4 630 637 |
institution |
Open Polar |
collection |
Czech Academy of Sciences: dKNAV |
op_collection_id |
ftczechacademysc |
language |
English |
topic |
obecná botanika general botany calcium-binding protein chilling stress chlorophyll fluorescence electrolyte leakage 2 581 |
spellingShingle |
obecná botanika general botany calcium-binding protein chilling stress chlorophyll fluorescence electrolyte leakage 2 581 Zhang, T. J. Pan, L. J. Huang, Qingrong Zhu, L. H. Yang, N. Peng, C. L. Chen, L. B. Overexpression of calmodulin gene fragment from Antarctic notothenioid fish improves chilling tolerance in Nicotiana benthamiana |
topic_facet |
obecná botanika general botany calcium-binding protein chilling stress chlorophyll fluorescence electrolyte leakage 2 581 |
description |
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 |
author |
Zhang, T. J. Pan, L. J. Huang, Qingrong Zhu, L. H. Yang, N. Peng, C. L. Chen, L. B. |
author_facet |
Zhang, T. J. Pan, L. J. Huang, Qingrong Zhu, L. H. Yang, N. Peng, C. L. Chen, L. B. |
author_sort |
Zhang, T. J. |
title |
Overexpression of calmodulin gene fragment from Antarctic notothenioid fish improves chilling tolerance in Nicotiana benthamiana |
title_short |
Overexpression of calmodulin gene fragment from Antarctic notothenioid fish improves chilling tolerance in Nicotiana benthamiana |
title_full |
Overexpression of calmodulin gene fragment from Antarctic notothenioid fish improves chilling tolerance in Nicotiana benthamiana |
title_fullStr |
Overexpression of calmodulin gene fragment from Antarctic notothenioid fish improves chilling tolerance in Nicotiana benthamiana |
title_full_unstemmed |
Overexpression of calmodulin gene fragment from Antarctic notothenioid fish improves chilling tolerance in Nicotiana benthamiana |
title_sort |
overexpression of calmodulin gene fragment from antarctic notothenioid fish improves chilling tolerance in nicotiana benthamiana |
url |
https://kramerius.lib.cas.cz/view/uuid:0cbb9a33-70ee-4e5a-986a-cf1eec1f15ae https://doi.org/10.1007/s11099-016-0682-z |
op_coverage |
630-637 |
geographic |
Antarctic |
geographic_facet |
Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_relation |
https://kramerius.lib.cas.cz/view/uuid:0cbb9a33-70ee-4e5a-986a-cf1eec1f15ae issn:0300-3604 doi:10.1007/s11099-016-0682-z |
op_rights |
policy:public |
op_doi |
https://doi.org/10.1007/s11099-016-0682-z |
container_title |
Photosynthetica |
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55 |
container_issue |
4 |
container_start_page |
630 |
op_container_end_page |
637 |
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1793765369227247616 |