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Neofunctionalization of zona pellucida proteins enhances freeze-prevention in the eggs of Antarctic notothenioids.


ABSTRACT: The mechanisms by which the eggs of the Antarctic notothenioid fishes avoid freezing are not fully understood. Zona pellucida proteins (ZPs) are constituents of the chorion which forms a protective matrix surrounding the egg. Here we report occurrence of freezing temperature-related gene expansion and acquisition of unusual ice melting-promoting (IMP) activity in a family of Antarctic notothenioid ZPs (AnnotoZPs). Members of AnnotoZPs are shown to bind with ice and non-colligatively depress the melting point of a solution in a range of 0.26 to 0.65?°C at a moderate concentration. Eggs of zebrafishes expressing an AnnotoZP transgene show improved melting point depression and enhanced survival in freezing conditions. Mutational analyses in a representative AnnotoZP indicate the ZP domain and patches of acidic residues are essential structures for the IMP activity. AnnotoZPs, therefore, represent a group of macromolecules that prevent freezing by a unique ZP-ice interaction mechanism distinct from the known antifreeze proteins.

SUBMITTER: Cao L 

PROVIDER: S-EPMC5059455 | biostudies-literature | 2016 Oct

REPOSITORIES: biostudies-literature

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Neofunctionalization of zona pellucida proteins enhances freeze-prevention in the eggs of Antarctic notothenioids.

Cao Lixue L   Huang Qiao Q   Wu Zhichao Z   Cao Dong-Dong DD   Ma Zhanling Z   Xu Qianghua Q   Hu Peng P   Fu Yanxia Y   Shen Yu Y   Chan Jiulin J   Zhou Cong-Zhao CZ   Zhai Wanying W   Chen Liangbiao L  

Nature communications 20161004


The mechanisms by which the eggs of the Antarctic notothenioid fishes avoid freezing are not fully understood. Zona pellucida proteins (ZPs) are constituents of the chorion which forms a protective matrix surrounding the egg. Here we report occurrence of freezing temperature-related gene expansion and acquisition of unusual ice melting-promoting (IMP) activity in a family of Antarctic notothenioid ZPs (AnnotoZPs). Members of AnnotoZPs are shown to bind with ice and non-colligatively depress the  ...[more]

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