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Bacterial Inner-membrane Display for Screening a Library of Antibody Fragments
Published on: October 15, 2016
FtsY binds to the Escherichia coli inner membrane via interactions with phosphatidylethanolamine and membrane
1Department of Biochemistry, McMaster University, Hamilton, Ontario L8N 3Z5, Canada.
Abstract:
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.
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