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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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:
2
581
Online Access:https://kramerius.lib.cas.cz/view/uuid:0cbb9a33-70ee-4e5a-986a-cf1eec1f15ae
https://doi.org/10.1007/s11099-016-0682-z
id ftczechacademysc:oai:kramerius.lib.cas.cz:uuid:0cbb9a33-70ee-4e5a-986a-cf1eec1f15ae
record_format openpolar
spelling 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
container_volume 55
container_issue 4
container_start_page 630
op_container_end_page 637
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