Super-resolution images of peptidoglycan remodelling enzymes at the division site of Escherichia coli
- Publication Type:
- Journal Article
- Citation:
- Current Genetics, 2019, 65 (1), pp. 99 - 101
- Issue Date:
- 2019-02-11
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| Filename | Description | Size | |||
|---|---|---|---|---|---|
| Söderström_Daley_Curr_Gen_2018.pdf | Published Version | 818.05 kB |
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© 2018, The Author(s). Bacterial cells need to divide. This process requires more than 30 different proteins, which gather at the division site. It is widely assumed that these proteins assemble into a macromolecular complex (the divisome), but capturing the molecular layout of this complex has proven elusive. Super-resolution microscopy can provide spatial information, down to a few tens of nanometers, about how the division proteins assemble into complexes and how their activities are co-ordinated. Herein we provide insight into recent work from our laboratories, where we used super-resolution gSTED nanoscopy to explore the molecular organization of FtsZ, FtsI and FtsN. The resulting images show that all three proteins form discrete densities organised in patchy pseudo-rings at the division site. Significantly, two-colour imaging highlighted a radial separation between FtsZ and FtsN, indicating that there is more than one type of macromolecular complex operating during division. These data provide a first glimpse into the spatial organisation of PG-synthesising enzymes during division in Gram-negative bacteria.
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