菌伴蛋白OBP域与氨基原蛋白的相互作用
Evgeniia V Leisi1, Darya V Zyurkalova2, Uliana F Dzhus2
1Belozersky Research Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Leninskie Gory 1, Bld 40, 119991, Moscow, Russia; Faculty of Bioengineering and Bioinformatics, Lomonosov Moscow State University, Leninskie Gory 1, Bld 73, 119991, Moscow, Russia.
Archives of biochemistry and biophysics
|June 2, 2025
概括
细菌病毒的沙佩罗宁,比如来自Pseudomonas fluorescens的OBP,可以防止粉样蛋白的形成. 即使没有角域,OBP仍然保持功能,结合并防止像α-synuclein这样的蛋白质的纤维化.
科学领域:
- * 分子生物学 * 分子生物学
- * 蛋白质生物化学 * 蛋白质生物化学
- * 病毒学 病毒学
背景情况:
- * 细菌病毒编码具有独特结构的GroEL-like chaperonins.
- *I组和II组的沙佩罗宁的特征很好,但病毒变异仍然不太了解.
- *来自Pseudomonas fluorescens菌OBP的单环沙佩罗宁为研究沙佩罗宁功能提供了一个独特的模型.
研究的目的:
- * 为了研究在OBP chaperonin中的顶点域 (AD) 的功能意义.
- * 确定AD删除对OBP的结构,组合和ATPase活性的影响.
- * 评估OBP及其变体在防止蛋白质聚合和粉样蛋白形成方面的作用.
主要方法:
- *删除变异的构建和表征:孤立的顶峰域 (AD) 和没有顶峰域的沙佩罗宁 (OBPΔAD).
- *对野生型OBP和OBPΔAD的结构完整性,heptameric组合和ATPase活性进行分析.
- *体外试验评估菌体内素对热聚合的保护作用和对粉样蛋白 (α-synuclein,蛋白) 纤维化的影响.
主要成果:
- *删除顶端域 (OBPΔAD) 稍微破坏了结构的稳定性,但保持了heptameric组合和ATPase活性.
- * OBPΔAD,在ATP的存在下,保护内溶素免受聚合,并促进α-synuclein和蛋白纤维化.
- * OBPΔAD 和分离的顶点域 (AD) 独立于ATP结合α-synuclein单体,防止自发动.
结论:
- * 基域对于OBP的heptameric组合,ATPase活性或基本伴侣功能来说并不重要.
- * 基质结合可以发生在OBP的内部腔内,即使没有顶峰域.
- * OBP chaperonins,特别是它们的核心结构,在调节氨基原蛋白的病理转化方面发挥着作用.
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