Structural dynamics of RbmA governs plasticity of Vibrio cholerae biofilms
Structural dynamics of RbmA governs plasticity of Vibrio cholerae biofilms
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DOI：
10.7554/elife.26163
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发表时间：
2017-08-01
期刊：
影响因子：
7.7
通讯作者：
Yildiz, Fitnat H.
中科院分区：
文献类型：
--
作者：
Fong, Jiunn C. N.;Rogers, Andrew;Yildiz, Fitnat H.
生物膜的形成是霍乱弧菌感染循环的关键。弧菌胞外多糖（VPS）和基质蛋白RbmA、Bap 1和RbmC是生物膜结构发展所必需的。我们证明了RbmA直接结合VPS，并在其第一个纤连蛋白III型（FnIII-1）结构域中使用二元结构开关来控制RbmA结构动力学和VPS依赖的高阶结构的形成。FnIII-1中的结构开关调节与FnIII-2结构域的反式相互作用，导致开放（单体）或封闭（二聚体）界面。RbmA在打开和关闭状态之间切换的能力对于霍乱弧菌生物膜形成是重要的，因为具有锁定在两种状态中的任一种的开关的RbmA变体导致具有改变的架构和结构完整性的生物膜。
Biofilm formation is critical for the infection cycle of Vibrio cholerae. Vibrio exopolysaccharides (VPS) and the matrix proteins RbmA, Bap1 and RbmC are required for the development of biofilm architecture. We demonstrate that RbmA binds VPS directly and uses a binary structural switch within its first fibronectin type III (FnIII-1) domain to control RbmA structural dynamics and the formation of VPS-dependent higher -order structures. The structural switch in FnIII-1 regulates interactions in trans with the FnIII-2 domain, leading to open (monomeric) or closed (dimeric) interfaces. The ability of RbmA to switch between open and closed states is important for V. cholerae biofilm formation, as RbmA variants with switches that are locked in either of the two states lead to biofilms with altered architecture and structural integrity.