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Structure and functional analysis reveal an important regulated role of arginine kinase in Patinopecten yessoensis under low pH stress.
Aquatic Toxicology ( IF 4.1 ) Pub Date : 2020-02-19 , DOI: 10.1016/j.aquatox.2020.105452
Zujing Yang 1 , Xiaoting Huang 2 , Huan Liao 3 , Zhengrui Zhang 1 , Fanhua Sun 1 , Sihua Kou 1 , Zhenmin Bao 2
Affiliation  

Arginine kinase (AK), an important member of the phosphokinase family, is involved in temporal and spatial adenosine triphosphate (ATP) buffering systems. AK plays an important role in physiological function and metabolic regulations, in particular tissues with high and fluctuating energy demands. In present study, four AK genes were firstly identified from Yesso scallop (Patinopecten yessoensis) genome, respectively named PyAK1-4. PyAKs have highly conserved structures with a six-exon/five-exon structure, except for PyAK3. PyAK3 contains an unusual two-domain structure and a "bridge intron" between the two domains, which may originate from gene duplication and subsequent fusion. Phylogenetic analysis showed that all PyAKs belonged to an AK supercluster together with other AK proteins from Mollusca, Platyhelminthes, Arthropoda, and Nematode. A transcriptome database demonstrated that PyAK3 and PyAK4 were the main functional executors with high expression level during larval development and in adult tissues, while PyAK1 and PyAK2 were expressed at a low level. Furthermore, both PyAK2 and PyAK3 showed notably high expression in the male gonad, and PyAK4 was broadly expressed in almost all tissues with the highest level in striated muscle, indicating a tissue-specific expression pattern of PyAKs. In addition, quantitative real-time PCR results demonstrated that the expression of PyAK2, PyAK3 and PyAK4 were significantly upregulated in response to pH stress, especially in an extremely acidifying condition (pH 6.5), revealing the possible involvement of PyAKs in energetic homeostasis during environmental changes. Collectively, a comprehensive analysis of PyAKs was conducted in P. yessoensis. The diversity of PyAKs and their specific expression patterns promote a better understanding of energy metabolism in the growth, development and environmental response of P. yessoensis.

中文翻译:

结构和功能分析表明,在低pH胁迫下,精氨酸激酶在野参中的重要调节作用。

精氨酸激酶(AK)是磷酸激酶家族的重要成员,参与了时空三磷酸腺苷(ATP)缓冲系统。AK在生理功能和代谢调节中,特别是在能量需求高且波动的组织中,起着重要作用。在本研究中,首先从野扇贝(Patinopecten yessoensis)基因组中鉴定出四个AK基因,分别命名为PyAK1-4。PyAK具有高度保守的结构,具有六外显子/五外显子结构,但PyAK3除外。PyAK3包含一个不寻常的两个域结构和两个域之间的“桥内含子”,这可能源于基因复制和随后的融合。系统发育分析表明,所有PyAK与其他软体动物,软体动物,节肢动物,节肢动物,和线虫。转录组数据库显示,PyAK3和PyAK4是幼虫发育期间和成人组织中高表达水平的主要功能执行子,而PyAK1和PyAK2则低表达。此外,PyAK2和PyAK3在雄性腺中均表现出显着的高表达,并且PyAK4在横纹肌中具有最高水平的几乎所有组织中广泛表达,表明了PyAK的组织特异性表达模式。此外,实时定量PCR结果表明,PyAK2,PyAK3和PyAK4的表达在pH胁迫下显着上调,尤其是在极端酸化条件下(pH 6.5),这表明在环境中PyAKs可能参与了能量平衡。变化。总的来说,在野牛假单胞菌中对PyAKs进行了全面分析。PyAKs的多样性及其特定的表达方式促进了对能量代谢的了解,从而促进了P. yessoensis的生长。
更新日期:2020-02-20
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