中文摘要：肺炎支原体末端细胞器具有粘附和滑移的功能，该细胞器由至少11个亚结构组成。研究利用电子冷冻断层扫描技术分析滑移与粘膜功能的缺失与不同末端细胞器变异体结构变化的关系。研究分析了prkC、prpC、P200和HMW3突变体的11个亚结构，为进一步了解肺炎支原体细胞结构中末端细胞器蛋白的功能及复杂的细胞结果的功能提供了基础。
 
外文摘要：The Mycoplasma pneumoniae terminal organelle functions in adherence and gliding motility and is comprised of at least eleven substructures. We used electron cryotomography to correlate impaired gliding and adherence function with changes in architecture in diverse terminal organelle mutants. All eleven substructures were accounted for in the prkC, prpC and P200 mutants, and variably so for the HMW3 mutant. Conversely, no terminal organelle substructures were evident in HMW1 and HMW2 mutants. The P41 mutant exhibits a terminal organelle detachment phenotype and lacked the bowl element normally present at the terminal organelle base. Complementation restored this substructure, establishing P41 as either a component of the bowl element or required for its assembly or stability, and that this bowl element is essential to anchor the terminal organelle but not for leverage in gliding. Mutants II-3, III-4 and topJ exhibited a visibly lower density of protein knobs on the terminal organelle surface. Mutants II-3 and III-4 lack accessory proteins required for a functional adhesin complex, while the topJ mutant lacks a DnaJ-like co-chaperone essential for its assembly. Taken together, these observations expand our understanding of the roles of certain terminal organelle proteins in the architecture and function of this complex structure.
外文关键词：ACCESSORY PROTEIN HMW1; CO-CHAPERONE TOPJ; ATTACHMENT ORGANELLE; GLIDING MOTILITY; CYTADHERENCE PROTEINS; HUMAN PATHOGEN; TRITON SHELL; P1 ADHESIN; LOCALIZATION; HEMADSORPTION
作者：Krause, DC; Chen, SY; Shi, J; Jensen, AJ; Sheppard, ES; Jensen, GJ
作者单位：美国佐治亚大学
期刊名称：MOLECULAR MICROBIOLOGY
期刊影响因子：3.898
出版年份：2018
出版刊次：3
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