Journal article
Last but not least: new insights into how FtsN triggers constriction during Escherichiacoli cell division
Molecular microbiology, Vol.95(6), pp.903-909
03/01/2015
DOI: 10.1111/mmi.12925
PMID: 25571948
Abstract
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.
Details
- Title: Subtitle
- Last but not least: new insights into how FtsN triggers constriction during Escherichiacoli cell division
- Creators
- David S Weiss
- Resource Type
- Journal article
- Publication Details
- Molecular microbiology, Vol.95(6), pp.903-909
- Publisher
- Wiley Subscription Services, Inc
- DOI
- 10.1111/mmi.12925
- PMID
- 25571948
- ISSN
- 0950-382X
- eISSN
- 1365-2958
- Grant note
- name: The University of Iowa
- Language
- English
- Date published
- 03/01/2015
- Description audience
- Academic
- Academic Unit
- Microbiology and Immunology
- Record Identifier
- 9984001214702771
Metrics
24 Record Views