Abstract
The gene encoding a periplasmic pH 2·5 acid phosphatase (appA) from Escherichia coli was placed under the control of an inducible promoter and integrated into the chromosome of Myxococcus xanthus. The majority of the AppA protein synthesized in M. xanthus accumulated in the periplasm whereas about 30% was secreted into the medium. The kinetics of AppA secretion through the ‘outer envelopes’ (i.e. periplasm + outer membrane) were followed after AppA induction. The results suggest that AppA crosses these envelopes by a mechanism involving diffusion and show that the periplasmic accumulation of AppA and envelope permeability are decreased by mutations that decrease the secretion of native proteins in M. xanthus.
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