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Super-resolution images of peptidoglycan remodelling enzymes at the division site of Escherichia coli
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.ORCID iD: 0000-0002-6425-5059
Number of Authors: 32019 (English)In: Current Genetics, ISSN 0172-8083, E-ISSN 1432-0983, Vol. 65, no 1, p. 99-101Article, review/survey (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
2019. Vol. 65, no 1, p. 99-101
Keywords [en]
E. coli, Cell division, FtsZ, FtsI, FtsN, Peptidoglycan
National Category
Biological Sciences
Identifiers
URN: urn:nbn:se:su:diva-166765DOI: 10.1007/s00294-018-0869-xISI: 000456958800012PubMedID: 30056491OAI: oai:DiVA.org:su-166765DiVA, id: diva2:1296023
Available from: 2019-03-13 Created: 2019-03-13 Last updated: 2019-03-13Bibliographically approved

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Söderström, BillDaley, Daniel O.
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