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中国农学通报

中国农学通报 ›› 2013, Vol. 29 ›› Issue (22): 40-45.doi: 10.11924/j.issn.1000-6850.2013-0850

所属专题： 生物技术

• 林学 园艺 园林 • 上一篇    下一篇

松材线虫sHSP16A基因克隆及蛋白质结构研究

刘立宏 王峰 王步勇 马玲 杨洋 崔伟婵   

  • 收稿日期:2013-03-26 修回日期:2013-05-22 出版日期:2013-08-05 发布日期:2013-08-05
  • 基金资助:
    瑞典国际自然科学基金;高等学校博士学科点专项科研基金资助课题（博士点新教师基金资助项目）;东北林业大学校立基金

Gene Cloning and Protein Structure Implications of a sHSP16A from Bursaphelenchus xylophilus

  • Received:2013-03-26 Revised:2013-05-22 Online:2013-08-05 Published:2013-08-05

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摘要： 分子伴侣小热激蛋白（sHSPs）是线虫度过高温环境的关键因子。热激条件下，小热激蛋白参与细胞损伤的修复，在线虫生长和发育过程中发挥重要作用。本研究克隆到松材线虫小热激蛋白sHSP16A基因。sHSP16A具α-crystallin保守结构域“F-polar-R-polar-aromatic-x-L-P”序列和“I/L-x-I”序列，初步判断具备分子伴侣功能。Bx-sHSP16A与多个蛋白发生互作，深入研究这些蛋白有助于了解Bx-sHSP16A在应激反应路径中的作用。Bx-sHSP16A二聚体中A亚基的“I/L-x-I”序列可以嵌入B亚基的去水合位点，契合后氢键稳定，说明Bx-sHSP16A可以形成多聚体。在应激反应过程中，Bx-sHSP16A以多聚体形式发挥功能。

关键词: 分子生物学技术, 分子生物学技术

Abstract: The molecular chaperones of small heat shock proteins (sHSPs) are key components that contribute to nematode survival in higher temperatures stress response. In heat shock, the sHSPs help the cell survival by the way of cell repair. A Bursaphelenchus xylophilus sHSP16A gene, Bx-sHSP16A, were found and well studied. The sHSP16A conserved motif “F-polar-R-polar-aromatic-x-L-P” and “I/L-x-I” were found in Bx-sHSP16A. Bx-sHSP16A has the chaperonelike functions. Bx-sHSP16A interact with many proteins, well studies of those proteins will help us understand the pathway related with sHSPs. In the Bx-sHSP16A dimer, the C terminus` “I/L-x-I” of the subunit A binding with the groove of the subunit B. These results indicated that Bx-sHSP16As could form oligomer. The chaperone activity of the Bx-sHSP16As oligomer has been postulated to coincide with the exposure of hydrophobic interface sites after a temperature-regulated subunit exchange or dissociation of the oligomer.