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Membrane insertion mechanism and molecular assembly of the bacteriophage lysis toxin ΦX174‐E
Author(s) -
Mezhyrova Julija,
Martin Janosch,
Peetz Oliver,
Dötsch Volker,
Morgner Nina,
Ma Yi,
Bernhard Frank
Publication year - 2021
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.15642
Subject(s) - transmembrane domain , lysis , transmembrane protein , biophysics , bacteriophage , biochemistry , biology , escherichia coli , membrane , cell membrane , chemistry , microbiology and biotechnology , receptor , gene
Due to high toxicity in a wide range of Gram‐negative bacteria phage, ΦX174 is particularly interesting for medical applications. Our data support a revised two‐step activation model of the phage toxin ΦX174‐E by the bacterial chaperone SlyD. Sequential binding of SlyD to both ΦX174‐E domains prevents formation of an inactive conformation and catalyzes its membrane insertion. Within the membrane, ΦX174‐E forms oligomeric complexes, a potential prerequisite for lysis.