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Overexpression of phosphatidylglycerophosphate synthase restores protein translocation in a secG deletion mutant of Escherichia coli at low temperature
Author(s) -
V P Kontinen,
H Tokuda
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00378-m
Subject(s) - mutant , bacillus subtilis , chromosomal translocation , plasmid , escherichia coli , suppressor mutation , atp synthase , gene , biology , mutation , microbiology and biotechnology , chemistry , biochemistry , genetics , bacteria
The E. coli secG deletion mutant is unable to grow and is defective in protein translocation at low temperature. A gene of Bacillus subtilis , which is able to restore the growth of the deletion mutant at low temperature, was found as a multi‐copy suppressor. Sequencing of this gene revealed significant homology to E. coli pgsA , which encodes phosphatidylglycerophosphate synthase, an enzyme involved in acidic phospholipid synthesis. A plasmid carrying E. coli pgsA also restored the growth of the deletion mutant. Furthermore, protein translocation in the deletion mutant was stimulated when it harbored a plasmid carrying pgsA . A possible mechanism underlying the pgsA ‐dependent suppression of the secG deletion mutation is discussed.