Functional domain analysis of the Mycoplasma pneumoniae co-chaperone TopJ.

摘要: Colonization of conducting airways humans by the prokaryote Mycoplasma pneumoniae is mediated a differentiated terminal organelle important in cytadherence, gliding motility and cell division. TopJ predicted J-domain co-chaperone also having domains unique to mycoplasma proteins essential for function, as well stabilization protein P24, which required normal initiation formation. J-domains activate ATPase DnaK chaperones, facilitating peptide binding proper folding. We performed mutational analysis J-domain, central acidic proline-rich (APR) domain, C-terminal domain assessed phenotypic consequences when introduced into an M. topJ mutant. A derivative with amino acid substitutions canonical histidine-proline-aspartic motif restored P24 levels but not motility, morphology or consistent function. In contrast, derivatives APR deletions were less stable failed restore resulted morphology, intermediate cytadherence exceeding that wild-type cells. Results from immunofluorescence microscopy suggest both domains, motif, are critical localization organelle.