期刊
MOLECULAR MICROBIOLOGY
卷 95, 期 6, 页码 903-909出版社
WILEY-BLACKWELL
DOI: 10.1111/mmi.12925
关键词
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资金
- NIH HHS [P51 OD011132] Funding Source: Medline
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.
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