Structure and functional analysis reveal an important regulated role of arginine kinase in Patinopecten yessoensis under low pH stress

Highlights

• Four PyAKs were systematically identified and characterized from Patinopecten yessoensis.

• Phylogenetic analysis suggested an unusual two-domain AK (PyAK3) originated from gene duplication and fusion.

• PyAK3 and PyAK4 were mainly functional AKs in healthy tissues and during different developmental stages.

• PyAK2, PyAK3 and PyAK4 played critical roles in ATP buffering systems under low pH stress.

Abstract

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.

Yang Z., Huang X., Li H., Zhang Z., Sun F., Kou S. & Bao Z., 2020. Structure and functional analysis reveal an important regulated role of arginine kinase in Patinopecten yessoensis under low pH stress. Aquatic Toxicology 222: 105452. doi: 10.1016/j.aquatox.2020.105452. Article (subscription required).


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