Antifreeze protein from Ammopiptanthus nanus functions in temperature-stress through domain A

Abstract Temperature stress restricts plant growth and development. Antifreeze protein (AFP) can improve plants antifreeze ability. In our previous study, the AnAFP gene cloned from Ammopiptanthus nanus was confirmed to be an excellent candidate enhancing plant cold resistance. But, AnAFP protein sh...

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Autores principales: HaoQiang Yu, HongYing Zheng, Yuan Liu, QingQing Yang, WanChen Li, YuanYuan Zhang, FengLing Fu
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Publicado: Nature Portfolio 2021
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Acceso en línea:https://doaj.org/article/bf548b10cb2a45eca2333136b5e4643c
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spelling oai:doaj.org-article:bf548b10cb2a45eca2333136b5e4643c2021-12-02T18:27:47ZAntifreeze protein from Ammopiptanthus nanus functions in temperature-stress through domain A10.1038/s41598-021-88021-02045-2322https://doaj.org/article/bf548b10cb2a45eca2333136b5e4643c2021-04-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-88021-0https://doaj.org/toc/2045-2322Abstract Temperature stress restricts plant growth and development. Antifreeze protein (AFP) can improve plants antifreeze ability. In our previous study, the AnAFP gene cloned from Ammopiptanthus nanus was confirmed to be an excellent candidate enhancing plant cold resistance. But, AnAFP protein shared similar structures with KnS type dehydrins including K, N and S domains except ice crystal binding domain A. Here, we generated AnAFPΔA, AnAFPΔK, AnAFPΔN and AnAFPΔS, and transformed them into ordinary and cold sensitive strains of E. coli, and Arabidopsis KS type dehydrin mutant to evaluate their function. Expression of AnAFPΔA decreases cold and heat tolerance in E. coli, meanwhile, AnAFP enhances heat tolerance in Arabidopsis, suggesting that domain A is a thermal stable functional domain. AnAFP, AnAFPΔA and AnAFPΔS localize in whole cell, but AnAFPΔK and AnAFPΔN only localizes in nucleus and cytoplasm, respectively, exhibiting that K and N domains control localization of AnAFP. Likewise, K domain blocks interaction between AnAFP and AnICE1. The result of RT-qPCR showed that expression of AnAFP, AnICE1 and AnCBF genes was significantly induced by high-temperature, indicating that the AnAFP is likely regulated by ICE1-CBF-COR signal pathway. Taken together, the study provides insights into understanding the mechanism of AnAFP in response to temperature stress and gene resource to improve heat or cold tolerance of plants in transgenic engineering.HaoQiang YuHongYing ZhengYuan LiuQingQing YangWanChen LiYuanYuan ZhangFengLing FuNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-10 (2021)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
HaoQiang Yu
HongYing Zheng
Yuan Liu
QingQing Yang
WanChen Li
YuanYuan Zhang
FengLing Fu
Antifreeze protein from Ammopiptanthus nanus functions in temperature-stress through domain A
description Abstract Temperature stress restricts plant growth and development. Antifreeze protein (AFP) can improve plants antifreeze ability. In our previous study, the AnAFP gene cloned from Ammopiptanthus nanus was confirmed to be an excellent candidate enhancing plant cold resistance. But, AnAFP protein shared similar structures with KnS type dehydrins including K, N and S domains except ice crystal binding domain A. Here, we generated AnAFPΔA, AnAFPΔK, AnAFPΔN and AnAFPΔS, and transformed them into ordinary and cold sensitive strains of E. coli, and Arabidopsis KS type dehydrin mutant to evaluate their function. Expression of AnAFPΔA decreases cold and heat tolerance in E. coli, meanwhile, AnAFP enhances heat tolerance in Arabidopsis, suggesting that domain A is a thermal stable functional domain. AnAFP, AnAFPΔA and AnAFPΔS localize in whole cell, but AnAFPΔK and AnAFPΔN only localizes in nucleus and cytoplasm, respectively, exhibiting that K and N domains control localization of AnAFP. Likewise, K domain blocks interaction between AnAFP and AnICE1. The result of RT-qPCR showed that expression of AnAFP, AnICE1 and AnCBF genes was significantly induced by high-temperature, indicating that the AnAFP is likely regulated by ICE1-CBF-COR signal pathway. Taken together, the study provides insights into understanding the mechanism of AnAFP in response to temperature stress and gene resource to improve heat or cold tolerance of plants in transgenic engineering.
format article
author HaoQiang Yu
HongYing Zheng
Yuan Liu
QingQing Yang
WanChen Li
YuanYuan Zhang
FengLing Fu
author_facet HaoQiang Yu
HongYing Zheng
Yuan Liu
QingQing Yang
WanChen Li
YuanYuan Zhang
FengLing Fu
author_sort HaoQiang Yu
title Antifreeze protein from Ammopiptanthus nanus functions in temperature-stress through domain A
title_short Antifreeze protein from Ammopiptanthus nanus functions in temperature-stress through domain A
title_full Antifreeze protein from Ammopiptanthus nanus functions in temperature-stress through domain A
title_fullStr Antifreeze protein from Ammopiptanthus nanus functions in temperature-stress through domain A
title_full_unstemmed Antifreeze protein from Ammopiptanthus nanus functions in temperature-stress through domain A
title_sort antifreeze protein from ammopiptanthus nanus functions in temperature-stress through domain a
publisher Nature Portfolio
publishDate 2021
url https://doaj.org/article/bf548b10cb2a45eca2333136b5e4643c
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