Molecular characterization of Escherichia coli FtsE and FtsX

Mol Microbiol. 1999 Feb;31(3):983-93. doi: 10.1046/j.1365-2958.1999.01245.x.

Abstract

The genes ftsE and ftsX are organized in one operon together with ftsY. FtsY codes for the receptor of the signal recognition particle (SRP) that functions in targeting a subset of inner membrane proteins. We have found no indications for a structural relationship between FtsE/X and FtsY. Evidence is presented that FtsE and FtsX form a complex in the inner membrane that bears the characteristics of an ATP-binding cassette (ABC)-type transporter. FtsE is a hydrophilic nucleotide-binding protein that has a tendency to dimerize and associates with the inner membrane through an interaction with the integral membrane protein FtsX. An FtsE null mutant showed filamentous growth and appeared viable on high salt medium only, indicating a role for FtsE in cell division and/or salt transport.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • ATP-Binding Cassette Transporters*
  • Bacterial Proteins / analysis
  • Bacterial Proteins / genetics*
  • Cell Cycle Proteins / analysis
  • Cell Cycle Proteins / genetics*
  • Cell Survival
  • Cystic Fibrosis Transmembrane Conductance Regulator / analysis
  • Cystic Fibrosis Transmembrane Conductance Regulator / genetics*
  • Deoxyribodipyrimidine Photo-Lyase / metabolism
  • Dose-Response Relationship, Drug
  • Escherichia coli / genetics*
  • Escherichia coli Proteins*
  • Gene Expression Regulation, Bacterial
  • Immunoblotting
  • Mutagenesis
  • Precipitin Tests
  • Sodium Chloride / pharmacology
  • Sodium Compounds / pharmacology
  • Subcellular Fractions
  • Temperature
  • Time Factors
  • Urea / pharmacology

Substances

  • ATP-Binding Cassette Transporters
  • Bacterial Proteins
  • Cell Cycle Proteins
  • Escherichia coli Proteins
  • FtsX protein, E coli
  • FtsX protein, bacteria
  • Sodium Compounds
  • FtsE protein, E coli
  • Cystic Fibrosis Transmembrane Conductance Regulator
  • Sodium Chloride
  • Urea
  • Deoxyribodipyrimidine Photo-Lyase