Open AccessEscherichia coli pH 2.5 acid phosphatase and β‐lactamase TEM2 are secreted into the medium by Myxococcus xanthus
Author(s) -
Breton Annick M.,
GuespinMichel Janine F.
Publication year - 1987
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1987.tb02022.x
Subject(s) - myxococcus xanthus , periplasmic space , escherichia coli , extracellular , biochemistry , enzyme , biology , bacteria , microbiology and biotechnology , acid phosphatase , enterobacteriaceae , phosphatase , gene , mutant , genetics
The genes appA , coding for the periplasmic pH 2.5 acid phosphatase of Escherichia coli , and bla , borne by Tn1 coding for TEM2 β‐lactamase, another periplasmic enzyme in Gram‐negative bacteria, have been transferred and expressed in Myxococcus xanthus . The specified enzymes could be recovered from both cells and extracellular fluid. The pH 2.5 acid phosphatase was expressed in the same way as genuine extracellular proteins in Myxococcus . This activity was recovered throughout exponential growth and was modulated by mutations that affected he total amount of extracellular proteins. A possible mechanism for protein secretion in Myxococcus is discussed in view of these results.