Open AccessThe inner membrane protein YhdP modulates the rate of anterograde phospholipid flow in Escherichia coli
Author(s) -
Jacqueline Grimm,
Handuo Shi,
Wei Wang,
Angela M. Mitchell,
Ned S. Wingreen,
Kerwyn Casey Huang,
Thomas J. Silhavy
Publication year - 2020
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.2015556117
Subject(s) - bacteria , inner membrane , escherichia coli , bacterial outer membrane , mutant , membrane , microbiology and biotechnology , phospholipid , biology , biophysics , cell membrane , chemistry , biochemistry , gene , genetics
The outer membrane (OM) of Gram-negative bacteria is a selective permeability barrier that allows uptake of nutrients while simultaneously protecting the cell from harmful compounds. The basic pathways and molecular machinery responsible for transporting lipopolysaccharides (LPS), lipoproteins, and β-barrel proteins to the OM have been identified, but very little is known about phospholipid (PL) transport. To identify genes capable of affecting PL transport, we screened for genetic interactions with mlaA *, a mutant in which anterograde PL transport causes the inner membrane (IM) to shrink and eventually rupture; characterization of mlaA *-mediated lysis suggested that PL transport can occur via a high-flux diffusive flow mechanism. We found that YhdP, an IM protein involved in maintaining the OM permeability barrier, modulates the rate of PL transport during mlaA *-mediated lysis. Deletion of yhdP from mlaA * reduced the rate of IM transport to the OM by 50%, slowing shrinkage of the IM and delaying lysis. As a result, the weakened OM of ∆ yhdP cells was further compromised and ruptured before the IM during mlaA *-mediated death. These findings demonstrate the existence of a high-flux diffusive pathway for PL flow in Escherichia coli that is modulated by YhdP.