鞭毛
单核细胞增生李斯特菌
生物
抑制因子
微生物学
细胞生物学
运动性
功能(生物学)
基因
细菌
基因表达
遗传学
作者
So Yeon Cho,Hye-Won Na,Han Byeol Oh,Yun Mi Kwak,Wan Seok Song,Sun Cheol Park,Wook-Jong Jeon,Hongbaek Cho,Byung-Chul Oh,Jeongho Park,Seung Goo Kang,Geun-Shik Lee,Sung-il Yoon
摘要
The pathogenic Listeria monocytogenes bacterium produces the flagellum as a locomotive organelle at or below 30°C outside the host, but it halts flagellar expression at 37°C inside the human host to evade the flagellum-induced immune response. Listeria monocytogenes GmaR is a thermosensor protein that coordinates flagellar expression by binding the master transcriptional repressor of flagellar genes (MogR) in a temperature-responsive manner. To understand the regulatory mechanism whereby GmaR exerts the antirepression activity on flagellar expression, we performed structural and mutational analyses of the GmaR-MogR system. At or below 30°C, GmaR exists as a functional monomer and forms a circularly enclosed multidomain structure via an interdomain interaction. GmaR in this conformation recognizes MogR using the C-terminal antirepressor domain in a unique dual binding mode and mediates the antirepressor function through direct competition and spatial restraint mechanisms. Surprisingly, at 37°C, GmaR rapidly forms autologous aggregates that are deficient in MogR neutralization capabilities.
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