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鸡硒蛋白 N 的计算机分析:无 EF 手模体,CUGS-螺旋域在抗氧化保护中的作用。

In silico analysis of selenoprotein N (Gallus gallus): absence of EF-hand motif and the role of CUGS-helix domain in antioxidant protection.

机构信息

College of Veterinary Medicine, Northeast Agricultural University, Harbin 150030, P. R. China.

College of Pharmacy, Heilongjiang University of Chinese Medicine, Harbin 150040, P. R. China.

出版信息

Metallomics. 2021 Mar 8;13(3). doi: 10.1093/mtomcs/mfab004.

DOI:10.1093/mtomcs/mfab004
PMID:33693771
Abstract

Selenoprotein N (SEPN1) is critical to the normal muscular physiology. Mutation of SEPN1 can raise congenital muscular disorder in human. It is also central to maturation and structure of skeletal muscle in chicken. However, human SEPN1 contained an EF-hand motif, which was not found in chicken. And the biochemical and molecular characterization of chicken SEPN1 remains unclear. Hence, protein domains, transcription factors, and interactions of Ca2+ in SEPN1 were analyzed in silico to provide the divergence and homology between chicken and human in this work. The results showed that vertebrates' SEPN1 evolved from a common ancestor. Human and chicken's SEPN1 shared a conserved CUGS-helix domain with function in antioxidant protection. SEPN1 might be a downstream target of JNK pathway, and it could respond to multiple stresses. Human's SEPN1 might not combine with Ca2+ with a single EF-hand motif in calcium homeostasis, and chicken SEPN1 did not have the EF-hand motif in the prediction, indicating the EF-hand motif malfunctioned in chicken SEPN1.

摘要

硒蛋白 N(SEPN1)对正常的肌肉生理学至关重要。SEPN1 的突变会导致人类先天性肌肉疾病。它也是鸡骨骼肌成熟和结构的核心。然而,人类 SEPN1 含有一个 EF 手模体,而鸡中没有发现。鸡 SEPN1 的生化和分子特征仍然不清楚。因此,本研究通过计算机分析 SEPN1 的蛋白结构域、转录因子和 Ca2+的相互作用,以提供鸡和人类在这方面的差异和同源性。结果表明,脊椎动物的 SEPN1 由一个共同的祖先进化而来。人和鸡的 SEPN1 都有一个保守的 CUGS-螺旋结构域,具有抗氧化保护作用。SEPN1 可能是 JNK 途径的下游靶标,能够对多种应激作出反应。人类的 SEPN1 可能不会通过单个 EF 手模体与 Ca2+结合来维持钙稳态,而鸡 SEPN1 的预测中没有 EF 手模体,这表明 EF 手模体在鸡 SEPN1 中功能失常。

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