CAJ | 학술논문

　　分子伴侣小热激蛋白(sHSPs)是线虫度过高温环境的关键因子。为开发直接针对松材线虫的防治技术提供理论依据，对松材线虫小热激蛋白Bx-sHSP16A基因进行了研究。采用SL法进行基因全长克隆，STRING 9.0进行蛋白质互作网络分析，NAMD 2.9进行分子动力学模拟。本研究克隆到松材线虫小热激蛋白基因Bx-sHSP16A。Bx-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，去水合位点与多聚体聚合相关，Bx-sHSP16A以多聚体形式发挥分子伴侣功能。
　　분자반려소열격단백(sHSPs)시선충도과고온배경적관건인자。위개발직접침대송재선충적방치기술제공이론의거，대송재선충소열격단백Bx-sHSP16A기인진행료연구。채용SL법진행기인전장극륭，STRING 9.0진행단백질호작망락분석，NAMD 2.9진행분자동역학모의。본연구극륭도송재선충소열격단백기인Bx-sHSP16A。Bx-sHSP16A구α-crystallin보수결구역“F-polar-R-polar-aromatic-x-L-P”서렬화“I/L-x-I”서렬，초보판단구비분자반려공능。Bx-sHSP16A여다개단백발생호작，심입연구저사단백유조우료해Bx-sHSP16A재응격반응로경중적작용。Bx-sHSP16A이취체중A아기적“I/L-x-I”서렬가이감입B아기적거수합위점，계합후경건은정，설명Bx-sHSP16A가이형성다취체。재응격반응과정중，거수합위점여다취체취합상관，Bx-sHSP16A이다취체형식발휘분자반려공능。
The molecular chaperones of small heat shock proteins (sHSPs) are key components that contribute to nematode survival in higher temperatures stress response. To provide a theoretical basis for the control of Bursaphelenchus xylophilus, the small heat shock protein gene Bx-sHSP16A was studied. By the methods of nematode spliced leader the gene was cloned. The predicted interaction partners of STRING 9.0 were done to identify the protein-protein interactions. Molecular dynamics simulations were performed using NAMD 2.9. A B. 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 had the chaperonelike functions. Bx-sHSP16A interact with many proteins, well studies of those proteins would 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 had been postulated to coincide with the exposure of hydrophobic interface sites after a temperature-regulated subunit exchange or dissociation of the oligomer.