Cryo-electron microscopy reveals two distinct type IV pili assembled by the same bacterium
Cryo-electron microscopy reveals two distinct type IV pili assembled by the same bacterium
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DOI：
10.1038/s41467-020-15650-w
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发表时间：
2020-05-06
影响因子：
16.6
通讯作者：
Gold, Vicki A. M.
中科院分区：
文献类型：
--
作者：
Neuhaus, Alexander;Selvaraj, Muniyandi;Gold, Vicki A. M.
IV型皮利是细菌表面上的柔性细丝，由菌毛蛋白的螺旋组装体组成。它们参与细菌运动（抽搐），表面粘附，生物膜形成和DNA摄取（自然转化）。在这里，我们使用冷冻电子显微镜和质谱分析表明，细菌嗜热栖热菌产生两种形式的IV型菌毛（“宽”和“窄”），在结构和蛋白质组成不同。宽皮利由主要的毛蛋白PilA 4组成，而窄皮利由迄今为止未表征的毛蛋白组成，我们将其命名为PilA 5。功能性实验表明，PilA4是自然转化所必需的，而PilA5对于抽搐运动是重要的。IV型皮利是细菌表面上的柔性细丝，由菌毛蛋白的螺旋组装体组成。在这里，Neuhaus等人表明，嗜热栖热菌产生两种形式的IV型菌毛，在结构，蛋白质组成和功能上不同。
Type IV pili are flexible filaments on the surface of bacteria, consisting of a helical assembly of pilin proteins. They are involved in bacterial motility (twitching), surface adhesion, biofilm formation and DNA uptake (natural transformation). Here, we use cryo-electron microscopy and mass spectrometry to show that the bacterium Thermus thermophilus produces two forms of type IV pilus ('wide' and 'narrow'), differing in structure and protein composition. Wide pili are composed of the major pilin PilA4, while narrow pili are composed of a so-far uncharacterized pilin which we name PilA5. Functional experiments indicate that PilA4 is required for natural transformation, while PilA5 is important for twitching motility. Type IV pili are flexible filaments on the surface of bacteria, consisting of a helical assembly of pilin proteins. Here, Neuhaus et al. show that the bacterium Thermus thermophilus produces two forms of type IV pilus, differing in structure, protein composition, and function.