Open AccessCharacterization of two Pseudomonas aeruginosa mutants with defective secretion of extracellular proteins and comparison with other mutants
Author(s) -
Filloux Alain,
Murgier Maryse,
Wretlind Bengt,
Lazdunski Andrée
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.tb02017.x
Subject(s) - mutant , extracellular , elastase , periplasmic space , secretion , biology , alkaline phosphatase , biochemistry , lipase , microbiology and biotechnology , enzyme , gene , escherichia coli
We have isolated 2 new pleiotropic mutants of Pseudomonas aeruginosa strain PAO with defective secretion of extracellular proteins (Xcp mutants). One of these mutants was compared to 2 different, previously isolated secretion mutants. All had similar phenotypes and were unable to release at least 4 exoproteins (lipase, elastase, alkaline phosphatase, and phospholipase C), whilst alkaline protease was still secreted. The exoproteins appeared to be blocked in the periplasmic space. No difference in molecular weight was detected between cell‐bound forms of elastase and alkaline phosphatase in the different mutants and the corresponding extracellular forms from the wild‐type strain. Genetic mapping showed that the mutations were located in the 55′ region of the chromosome.