...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Cytoskeletal 'jellyfish'structure of Mycoplasma mopile
【24h】

Cytoskeletal 'jellyfish'structure of Mycoplasma mopile

机译：支原体流动的细胞骨架水母结构

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Mycoplasma mobile, a parasitic bacterium lacking a peptidoglycan layer, glides on solid surfaces in the direction of a membrane protrusion at a cell pole by a unique mechanism. Recently, we proposed a working model in which cells are propelled by leg proteins clustering at the protrusion's base. The legs repeatedly catch and release sialic acids on the solid surface, a motion that is driven by the force generated by ATP hydrolysis. Here, to clarify the subcellular structure supporting the gliding force and the cell shape, we stripped the membrane by Triton X-100 and identified a unique structure, designated the "jellyfish" structure. In this structure, an oval solid "bell" ≈ 235 wide and 155 nm long is filled with a 12-nm hexagonal lattice and connected to this structure are dozens of flexible "tentacles" that are covered with particles of 20-nm diameter at intervals of ≈ 30 nm. The particles appear to have 180° rotational symmetry and a dimple at the center. The relation of this structure to the gliding mechanism was suggested by its cellular localization and by analyses of mutants lacking proteins essential for gliding. We identified 10 proteins as the components by mass spectrometry and found that these do not show sequence similarities with other proteins of bacterial cy-toskeletons or the gliding proteins previously identified. Immuno-fluorescence and immunoelectron microscopy revealed that two components are localized at the bell and another that has the structure similar to the F_1-ATPase β subunit is localized at the tentacles.
机译：移动支原体，一种缺乏肽聚糖层的寄生细菌，通过独特的机制在固体表面上沿细胞极处的膜突出方向滑动。最近，我们提出了一个工作模型，其中腿蛋白聚集在突起的基部推动细胞。腿反复在固体表面捕获并释放唾液酸，该运动是由ATP水解产生的力驱动的。在这里，为了弄清支持滑行力和细胞形状的亚细胞结构，我们用Triton X-100剥离了膜，并确定了一个独特的结构，称为“水母”结构。在这种结构中，一个椭圆形的实心“钟形”部分（宽约235纳米，长155 nm）上填充有一个12 nm的六边形晶格，并且与该结构相连的是数十个柔性“触角”，这些触角被间隔为20 nm直径的粒子覆盖≈30 nm颗粒看起来具有180°旋转对称性，并且在中心处有一个凹窝。通过其细胞定位和缺乏对滑行必不可少的蛋白质的突变体的分析表明了这种结构与滑行机制的关系。我们通过质谱鉴定了10种蛋白质作为组成部分，发现这些蛋白质与细菌细胞骨架的其他蛋白质或先前鉴定的滑动蛋白质没有序列相似性。免疫荧光和免疫电子显微镜显示，两个组件位于钟形，另一个具有类似于F_1-ATPaseβ亚基的结构，位于触角。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号