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Journal of Bacteriology, August 2008, p. 5555-5566, Vol. 190, No. 16
0021-9193/08/$08.00+0     doi:10.1128/JB.00398-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

FtsW Is a Dispensable Cell Division Protein Required for Z-Ring Stabilization during Sporulation Septation in Streptomyces coelicolor ^,

Institute of Life Science, School of Medicine, Swansea University, Singleton Park, Swansea SA2 8PP, United Kingdom,¹ Nanotechnology Centre, School of Engineering, Swansea University, Singleton Park, Swansea SA2 8PP, United Kingdom,² John Innes Centre, Norwich Research Park, Colney, Norwich NR4 7UH, United Kingdom³

Received 20 March 2008/ Accepted 5 June 2008

The conserved rodA and ftsW genes encode polytopic membrane proteins that are essential for bacterial cell elongation and division, respectively, and each gene is invariably linked with a cognate class B high-molecular-weight penicillin-binding protein (HMW PBP) gene. Filamentous differentiating Streptomyces coelicolor possesses four such gene pairs. Whereas rodA, although not its cognate HMW PBP gene, is essential in these bacteria, mutation of SCO5302 or SCO2607 (sfr) caused no gross changes to growth and septation. In contrast, disruption of either ftsW or the cognate ftsI gene blocked the formation of sporulation septa in aerial hyphae. The inability of spiral polymers of FtsZ to reorganize into rings in aerial hyphae of these mutants indicates an early pivotal role of an FtsW-FtsI complex in cell division. Concerted assembly of the complete divisome was unnecessary for Z-ring stabilization in aerial hyphae as ftsQ mutants were found to be blocked at a later stage in cell division, during septum closure. Complete cross wall formation occurred in vegetative hyphae in all three fts mutants, indicating that the typical bacterial divisome functions specifically during nonessential sporulation septation, providing a unique opportunity to interrogate the function and dependencies of individual components of the divisome in vivo.

Published ahead of print on 13 June 2008.

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