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Minimal requirements for inhibition of MraY by lysis protein E from bacteriophage ΦX174
Author(s) -
Tanaka Shiho,
Clemons Jr William M.
Publication year - 2012
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.2012.08153.x
Subject(s) - lysis , biology , peptidoglycan , transmembrane domain , transmembrane protein , mutagenesis , lysin , bacteriophage , helix (gastropod) , spheroplast , biochemistry , microbiology and biotechnology , cell wall , membrane , escherichia coli , mutant , gene , ecology , receptor , snail
Summary The DNA phage ΦX174 encodes the integral membrane protein E whose expression leads to host cell lysis by inhibition of the peptidoglycan synthesis enzyme MraY. Here we use mutagenesis to characterize the molecular details of the E lysis mechanism. We find that a minimal 18‐residue region with the modified wild‐type sequences of the conserved transmembrane helix of E is sufficient to lyse host cells and that specific residues within and at the boundaries of this helix are important for activity. This suggests that positioning of the helix in the membrane is critical for interactions with MraY. We further characterize the interaction site of the transmembrane helix with MraY demonstrating E forms a stable complex with MraY. Triggering cell lysis by peptidoglycan synthesis inhibition is a traditional route for antimicrobial strategies. Understanding the mechanism of bacterial cell lysis by E will provide insights into new antimicrobial strategies using re‐engineered E peptides.