FtsY Binds to the Escherichia coli Inner Membrane via Interactions with Phosphatidylethanolamine and Membrane Proteins Academic Article uri icon

  • Overview
  • Research
  • Identity
  • Additional Document Info
  • View All


  • Targeting of many polytopic proteins to the inner membrane of prokaryotes occurs via an essential signal recognition particle-like pathway. FtsY, the Escherichia coli homolog of the eukaryotic signal recognition particle receptor alpha-subunit, binds to membranes via its amino-terminal AN domain. We demonstrate that FtsY assembles on membranes via interactions with phosphatidylethanolamine and with a trypsin-sensitive component. Both interactions are mediated by the AN domain of FtsY. In the absence of phosphatidylethanolamine, the trypsin-sensitive component is sufficient for binding and function of FtsY in the targeting of membrane proteins. We propose a two-step mechanism for the assembly of FtsY on the membrane similar to that of SecA on the E. coli inner membrane.


  • Millman, Jonathan S
  • Qi, Hai-Yan
  • Vulcu, Felicia
  • Bernstein, Harris D
  • Andrews, David W

publication date

  • July 2001