FtsN-like proteins are conserved components of the cell division machinery in proteobacteria
Article first published online: 21 APR 2009
© 2009 The Authors. Journal compilation © 2009 Blackwell Publishing Ltd
Volume 72, Issue 4, pages 1037–1053, May 2009
How to Cite
Möll, A. and Thanbichler, M. (2009), FtsN-like proteins are conserved components of the cell division machinery in proteobacteria. Molecular Microbiology, 72: 1037–1053. doi: 10.1111/j.1365-2958.2009.06706.x
- Issue published online: 8 MAY 2009
- Article first published online: 21 APR 2009
- Accepted 12 April, 2009.
In bacteria, cytokinesis is mediated by a ring-shaped multiprotein complex, called divisome. While some of its components are widely conserved, others are restricted to certain bacterial lineages. FtsN is the last essential cell division protein to localize to the division septum in Escherichia coli and is poorly conserved outside the enteric bacteria. We have identified a homologue of FtsN in the α-proteobacterium Caulobacter crescentus and show that it is essential for cell division. C. crescentus FtsN is recruited to the divisome significantly after cell division initiates and remains associated with the new cell poles after cytokinesis is finished. All determinants necessary for localization and function are located in a largely unstructured periplasmic segment of the protein. Its conserved SPOR-domain, by contrast, is dispensable for cytokinesis, although it supports targeting of FtsN to the division site. Interestingly, the SPOR-domain is recruited to the division plane when produced in isolated form and retains its localization potential in a heterologous host background. Searching for proteins that share the characteristic features of FtsN from E. coli and C. crescentus, we identified FtsN-like cell division proteins in β- and δ-proteobacteria, suggesting that FtsN is widespread among bacteria, albeit highly variable at the sequence level.