Overexpression of gnsA, a multicopy suppressor of the secG null mutation, increases acidic phospholipid contents by inhibiting phosphatidylethanolamine synthesis at low temperatures

J Bacteriol. 2004 Sep;186(17):5968-71. doi: 10.1128/JB.186.17.5968-5971.2004.

Abstract

GnsA overproduction was previously found to suppress both the secG null mutation and the fabA6 mutation in Escherichia coli by increasing the unsaturated fatty acid contents. We report here that it also increased the acidic phospholipid contents at 20 degrees C but not at 37 degrees C. GnsA overproduction at 20 degrees C specifically inhibited phosphatidylethanolamine synthesis and therefore caused the increase in the proportion of acidic phospholipids.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Escherichia coli / cytology
  • Escherichia coli / genetics*
  • Escherichia coli / metabolism*
  • Escherichia coli Proteins / genetics
  • Escherichia coli Proteins / metabolism*
  • Escherichia coli Proteins / physiology
  • Fatty Acid Synthase, Type II
  • Fatty Acids, Unsaturated / analysis
  • Genes, Bacterial*
  • Hydro-Lyases / genetics
  • Hydro-Lyases / physiology
  • Membrane Proteins / genetics
  • Membrane Proteins / physiology
  • Phosphatidylethanolamines / biosynthesis*
  • Phosphatidylethanolamines / genetics
  • Phospholipids / analysis*
  • Phospholipids / biosynthesis
  • SEC Translocation Channels
  • Temperature

Substances

  • Escherichia coli Proteins
  • Fatty Acids, Unsaturated
  • GnsA protein, E coli
  • Membrane Proteins
  • Phosphatidylethanolamines
  • Phospholipids
  • SEC Translocation Channels
  • SecG protein, E coli
  • phosphatidylethanolamine
  • Hydro-Lyases
  • 3-hydroxyacyl-(acyl-carrier-protein) dehydratase
  • Fatty Acid Synthase, Type II