SUPPRESSION OF FTSH MUTANT PHENOTYPES BY OVERPRODUCTION OF MOLECULAR CHAPERONES

Decreased intracellular levels of FtsH, a membrane-bound ATPase, led t o retardation of growth and protein export, as well as to an abnormal translocation of alkaline phosphatase that had been attached to a cyto plasmic domain of a multispanning membrane protein, SecY. The last phe notype is designated Std (stop transfer defective). In this study, we examined the effects of overproduction of some molecular chaperones on the phenotypes of ftsH mutants. The growth retardation was partially suppressed by overproduction of GroEL/GroES (Hsp60/Hsp10) or HtpG (Hsp 90), although these chaperones could not totally substitute for FtsH. Overproduction of HtpG specifically alleviated the Std phenotype, whil e that of GroEL/GroES alleviated the protein export defect of ftsH mut ants. These results suggest that FtsH functions can be somehow compens ated for when the cellular concentrations of some molecular chaperones increase.