Overexpression of phosphatidylglycerophosphate synthase restores protein translocation in a secG deletion mutant of Escherichia coli at low temperature

FEBS Lett. 1995 May 8;364(2):157-60. doi: 10.1016/0014-5793(95)00378-m.


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.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacillus subtilis / genetics
  • Bacterial Proteins / genetics*
  • Bacterial Proteins / metabolism*
  • Base Sequence
  • Biological Transport, Active
  • DNA, Bacterial / genetics
  • Escherichia coli / genetics*
  • Escherichia coli / growth & development
  • Escherichia coli / metabolism*
  • Escherichia coli Proteins*
  • Gene Deletion
  • Gene Expression
  • Genes, Bacterial
  • Membrane Proteins / genetics*
  • Molecular Sequence Data
  • SEC Translocation Channels
  • Sequence Homology, Amino Acid
  • Suppression, Genetic
  • Temperature
  • Transferases (Other Substituted Phosphate Groups) / genetics*


  • Bacterial Proteins
  • DNA, Bacterial
  • Escherichia coli Proteins
  • Membrane Proteins
  • SEC Translocation Channels
  • SecG protein, E coli
  • Transferases (Other Substituted Phosphate Groups)
  • CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase

Associated data

  • GENBANK/D50064
  • GENBANK/U56238