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Updated: Jul 4, 2026

Visual and Microscopic Evaluation of Streptomyces Developmental Mutants
Published on: September 12, 2018
FtsW is a dispensable cell division protein required for Z-ring stabilization during sporulation septation in
Bhavesh V Mistry1, Ricardo Del Sol, Chris Wright
1Institute of Life Science, School of Medicine, Swansea University, Singleton Park, Swansea SA2 8PP, United Kingdom.
Abstract:
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.
Insights
Bacterial cell division relies on the FtsW-FtsI complex for sporulation septum formation in Streptomyces coelicolor. This complex is crucial for Z-ring stabilization during aerial hyphae division.
Area of Science:
- Microbiology
- Cell Biology
- Bacterial Genetics
Background:
- The rodA and ftsW genes encode essential membrane proteins for bacterial cell elongation and division, respectively.
- These genes are typically linked with cognate class B high-molecular-weight penicillin-binding protein (HMW PBP) genes.
- Streptomyces coelicolor exhibits four such gene pairs, with rodA being essential, unlike its cognate HMW PBP gene.
Purpose of the Study:
- To investigate the roles of ftsW and its cognate ftsI gene in Streptomyces coelicolor cell division.
- To determine the function of the FtsW-FtsI complex in sporulation septation and Z-ring formation.
- To explore the specific involvement of the bacterial divisome in nonessential sporulation septation.
Main Methods:
- Gene disruption of ftsW and ftsI in Streptomyces coelicolor.
- Analysis of cell division and septum formation in vegetative and aerial hyphae.
- Microscopic observation of FtsZ ring polymerization and stabilization.
Main Results:
- Disruption of ftsW or ftsI blocked sporulation septum formation in aerial hyphae.
- Mutants showed an inability of FtsZ polymers to form rings, indicating a pivotal role for the FtsW-FtsI complex.
- ftsQ mutants were blocked later in septum closure, and vegetative hyphae completed cross-wall formation in all tested mutants.
Conclusions:
- The FtsW-FtsI complex plays a critical role in the early stages of sporulation septum formation and Z-ring stabilization in aerial hyphae.
- The bacterial divisome functions specifically during nonessential sporulation septation in Streptomyces coelicolor.
- This system allows for in vivo interrogation of individual divisome component functions and dependencies.
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