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Last but not least: new insights into how FtsN triggers constriction during E scherichia coli cell division
Author(s) -
Weiss David S.
Publication year - 2015
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/mmi.12925
Subject(s) - periplasmic space , peptidoglycan , cytoplasm , microbiology and biotechnology , biology , cell envelope , cell division , biochemistry , cell , cell wall , escherichia coli , gene
Summary The arrival of FtsN at the division site triggers synthesis of septal peptidoglycan and constriction of the cell envelope. New findings are changing our view of how this happens. Binding of FtsN 's cytoplasmic domain to a protein named FtsA recruits a small amount of FtsN to the division site earlier than previously recognized. The ability of FtsA to interact with FtsN is regulated by the ZipA protein. The FtsN – FtsA interaction pushes FtsA into an ‘on’ conformation that activates the machinery for peptidoglycan synthesis. In addition, a small region of FtsN 's periplasmic domain appears to interact with the FtsQLB complex, pushing it into an ‘on’ state that also triggers synthesis of peptidoglycan. Thus, FtsN allosterically activates peptidoglycan synthesis by two pathways, one in the cytoplasm and involving FtsA , and the other in the periplasm and involving FtsQLB .