Stability and subcellular localization of cytadherence- associated proteinP65 in Mycoplasma pneumoniae

The surface protein P65 is a constituent of the Mycoplasma pneumoniae cytos keleton and is present at reduced levels in mutants lacking the cytadherenc e accessory protein HMW2. Pulse-chase studies demonstrated that P65 is subj ect to accelerated turnover in the absence of HMW2. P65 was also less abund ant in noncytadhering mutants lacking HMW1 or P30 but was present at wild-t ype levels in mutants lacking proteins A, B, C, and P1. P65 exhibited a pol ar localization like that in wild-type M. pneumoniae in all mutants having normal levels of HMW1 and HMW2. Partial or complete loss of these proteins, however, correlated with severe reduction in the P65 level and the inabili ty to localize P65 properly.