FTSZ AND MYCOPLASMA PNEUMONIAE CELL DIVISION

大多数有壁原核生物的细胞分裂蛋白在无壁细菌肺炎支原体中是不存在的，除了FtsZ的一个相当不同的同源物，它在其他生物的细胞分裂位点形成一个环。 我们认为，如果M。Pneumoniae FtsZ在胞质分裂中起作用，它必须独立于其他生物体中与FtsZ相关的其他活性，可能与不同的蛋白质组相关;因此，FtsZ必须具有新的性质。 为了开始阐明M. pneumoniae的FtsZ同源物在分子水平上与M. pneumoniae的重组质粒将在大肠杆菌中表达并从大肠杆菌纯化。 纯化的蛋白质将原位定位于支原体细胞中。 此外，纯化的重组FtsZ蛋白将被表征为核苷酸亲和力、核苷酸水解动力学及其聚合，以便能够将这些性质与其他生物体的FtsZ同系物的性质进行比较。 最后，与M.将寻找肺炎FtsZ。

Most of the cell division proteins of walled prokaryotes are absent in the wall-less bacterium Mycoplasma pneumoniae, with the exception of a considerably divergent homolog of FtsZ, which forms a ring at the cell division site in other organisms. We reason that if M. pneumoniae FtsZ functions in cytokinesis, it must do so independently of the other activities that are associated with FtsZ in other organisms, perhaps in association with a different set of proteins; M. pneumoniae FtsZ therefore must have novel properties. In order to begin to elucidate the mechanism of M. pneumoniae cell division at the molecular level, the FtsZ homolog of M. pneumoniae will be expressed in and purified from E coli. The purified protein will be localized in situ in mycoplasma cells. Furthermore, purified recombinant FtsZ protein will be characterized for nucleotide affinity, kinetics of nucleotide hydrolysis, and its polymerization, in order to enable comparison of these properties with those of the FtsZ homologs of other organisms. Finally, proteins that interact with M. pneumoniae FtsZ will be sought.