Identification and sequence analyses of the gliding machinery proteins from Mycoplasma mobile
Identification and sequence analyses of the gliding machinery proteins from Mycoplasma mobile
复制标题
移动支原体滑动机械蛋白的鉴定和序列分析
DOI：
10.1038/s41598-020-60535-z
复制
发表时间：
2020
影响因子：
4.6
通讯作者：
Miyata M
中科院分区：
文献类型：
--
作者：
Tulum I;Kimura K;Miyata M
移动的支原体是一种鱼类病原菌，它在宿主细胞上表现出其特有的基于ATP水解的滑行运动。使这种运动性的特殊蛋白质机制由表面和内部蛋白质复合物组成。四种蛋白质，MMOB 1630、1660、1670和4860构成内部复合物，包括F型ATP酶/合酶α和β亚基的旁系同源物。在本研究中，细胞定位的候选滑行机制蛋白，MMOBs 1620，1640，1650，和5430进行了研究，通过使用全内反射荧光显微镜系统后，这些蛋白质与增强型黄色荧光蛋白（EYFP）标记。他们表达融合蛋白MMOB 1620-EYFP的mobilestrain表现出降低的细胞结合活性，而表达与EYFP融合的MMOB 1640的菌株表现出增加的滑动速度，表明这些蛋白参与了滑动机制。基于基因组序列，我们分析了四种滑行支原体的内部和表面复合物蛋白的序列保守性。与表面复合物相比，内部复合物中的蛋白质更保守，表明表面复合物根据宿主进行修饰。分析表明，内部滑动复合体是高度保守的，可能是由于它在运动机制中的作用。
Mycoplasma mobile, a fish pathogen, exhibits its own specialized gliding motility on host cells based on ATP hydrolysis. The special protein machinery enabling this motility is composed of surface and internal protein complexes. Four proteins, MMOBs 1630, 1660, 1670, and 4860 constitute the internal complex, including paralogs of F-type ATPase/synthase α and β subunits. In the present study, the cellular localisation for the candidate gliding machinery proteins, MMOBs 1620, 1640, 1650, and 5430 was investigated by using a total internal reflection fluorescence microscopy system after tagging these proteins with the enhanced yellow fluorescent protein (EYFP). TheM. mobilestrain expressing a fusion protein MMOB1620-EYFP exhibited reduced cell-binding activity and a strain expressing MMOB1640 fused with EYFP exhibited increased gliding speed, showing the involvement of these proteins in the gliding mechanism. Based on the genomic sequences, we analysed the sequence conservativity in the proteins of the internal and the surface complexes from four gliding mycoplasma species. The proteins in the internal complex were more conserved compared to the surface complex, suggesting that the surface complex undergoes modifications depending on the host. The analyses suggested that the internal gliding complex was highly conserved probably due to its role in the motility mechanism.