食品科学 ›› 2024, Vol. 45 ›› Issue (3): 1-8.doi: 10.7506/spkx1002-6630-20230323-228

• 基础研究 •    下一篇

牛HSPA6蛋白特性分析及蛋白互作网络构建

胡丽筠,马旭华,李亚蕾,罗瑞明   

  1. (宁夏大学食品科学与工程学院,宁夏 银川 750000)
  • 出版日期:2024-02-15 发布日期:2024-03-06
  • 基金资助:
    国家自然科学基金地区科学基金项目(32160535);宁夏回族自治区重点研发项目(2017BY068)

Characteristics Analysis of Bovine HSPA6 Protein and Construction of Protein Interaction Network

HU Lijun, MA Xuhua, LI Yalei, LUO Ruiming   

  1. (School of Food Science and Engineering, Ningxia University, Yinchuan 750000, China)
  • Online:2024-02-15 Published:2024-03-06

摘要: 通过构建牛热休克蛋白A6(heat shock protein A6,HSPA6)序列与其他生物的系统进化树,以及运用生物信息学方法分析牛HSPA6蛋白的基本理化性质、亲疏水性等,并结合蛋白互作网络,探究牛HSPA6基因编码蛋白的结构和功能特性。结果显示,牛HSPA6蛋白与羊、长江江豚等哺乳动物的氨基酸序列相似性较高;牛HSPA6蛋白分子质量为70 570.64 u,理论等电点为5.66,为酸性亲水性蛋白,无跨膜结构和信号肽;可能存在11 个得分>0.900的磷酸化位点,与N-糖基化激活位点可能位于后端碱基;牛HSPA6蛋白是一种主要由40.38%的α-螺旋和33.65%的无规卷曲组成的二级结构相对稳定的蛋白质,包含N-端核苷酸结合域和C-端多肽结合域两个主要的结构域,主要在细胞质中发挥作用;蛋白质互作网络构建结果显示,牛HSPA6蛋白主要与BAG1、DNAJA4、DNAJB1、DNAJC2等蛋白发生互作,参与腺苷酸交换因子活性、ATP酶调节活性、伴侣绑定等,表明牛HSPA6蛋白在牛机体能量代谢等过程中发挥潜在生物学功能。这些多重生物信息学分析为深入探讨牛HSPA6蛋白对肉品质的影响机制提供了理论依据。

关键词: 牛;热休克蛋白A6;结构特点;功能特性;蛋白质互作网络

Abstract: In this study, a phylogenetic tree was constructed using bovine heat shock protein A6 (HSPA6) sequences and those of other organisms, and bioinformatic methods were used to analyze the basic physicochemical properties and hydrophilicity of bovine HSPA6 protein. Meanwhile, a protein interaction network was constructed to investigate the structural and functional properties of the protein encoded by the HSPA6 gene. The results showed that bovine HSPA6 protein had high similarity in amino acid sequence with those of sheep, Yangtze finless porpoise and other mammals. The molecular mass of bovine HSPA6 protein was 70 570.64 u, the theoretical isoelectric point was 5.66, and it was an acidic hydrophilic protein without transmembrane structure or signal peptide. Bovine HSPA6 protein may have 11 phosphorylation sites with score greater than 0.900 and N-glycosylation sites at the terminal bases, and it was a relatively stable protein with a secondary structure consisting mainly of 40.38% α-helix and 33.65% random coil, containing two major structural domains, the N-terminal nucleotide-binding domain and the C-terminal peptide-binding domain, which played a role in the cytoplasm. The constructed protein network showed that bovine HSPA6 protein mainly interacted with BAG1, DNAJA4, DNAJB1 and DNAJC2, and was involved in the activity of adenylate exchange factors, ATPase activity and chaperone binding, indicating that the HSPA6 protein exerted a potential function in biological processes such as energy metabolism in the bovine organism. These multiple bioinformatic analyses provide a theoretical basis for an in-depth investigation of the mechanism of the effect of bovine HSPA6 protein on meat quality.

Key words: Bos taurus; heat shock protein A6; structural features; functional properties; protein interaction network

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