Coordinated disassembly of the divisome complex in Escherichia coli.

Söderström, B; Mirzadeh, K; Toddo, S; von Heijne, G; Skoglund, U; Daley, DO

Coordinated disassembly of the divisome complex in Escherichia coli.

Söderström, B Mirzadeh, K Toddo, S von Heijne, G Skoglund, U Daley, DO

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Publisher:: WILEY
Publication Type:: Journal Article
Citation:: Mol Microbiol, 2016, 101, (3), pp. 425-438
Issue Date:: 2016-08

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Field	Value	Language
dc.contributor.author	Söderström, B
dc.contributor.author	Mirzadeh, K
dc.contributor.author	Toddo, S
dc.contributor.author	von Heijne, G
dc.contributor.author	Skoglund, U
dc.contributor.author	Daley, DO
dc.date.accessioned	2022-03-31T06:37:39Z
dc.date.available	2016-04-18
dc.date.available	2022-03-31T06:37:39Z
dc.date.issued	2016-08
dc.identifier.citation	Mol Microbiol, 2016, 101, (3), pp. 425-438
dc.identifier.issn	0950-382X
dc.identifier.issn	1365-2958
dc.identifier.uri	http://hdl.handle.net/10453/155794
dc.description.abstract	The divisome is the macromolecular complex that carries out cell division in Escherichia coli. Every generation it must be assembled, and then disassembled so that the sequestered proteins can be recycled. Whilst the assembly process has been well studied, virtually nothing is known about the disassembly process. In this study, we have used super-resolution SIM imaging to monitor pairs of fluorescently tagged divisome proteins as they depart from the division septum. These simple binary comparisons indicated that disassembly occurs in a coordinated process that consists of at least five steps: [FtsZ, ZapA] ⇒ [ZipA, FtsA] ⇒ [FtsL, FtsQ] ⇒ [FtsI, FtsN] ⇒ [FtsN]. This sequence of events is remarkably similar to the assembly process, indicating that disassembly follows a first-in, first-out principle. A secondary observation from these binary comparisons was that FtsZ and FtsN formed division rings that were spatially separated throughout the division process. Thus the data indicate that the divisome structure can be visualized as two concentric rings; a proto-ring containing FtsZ and an FtsN-ring.
dc.format	Print-Electronic
dc.language	eng
dc.publisher	WILEY
dc.relation.ispartof	Mol Microbiol
dc.relation.isbasedon	10.1111/mmi.13400
dc.rights	info:eu-repo/semantics/closedAccess
dc.subject	06 Biological Sciences, 07 Agricultural and Veterinary Sciences, 11 Medical and Health Sciences
dc.subject.classification	Microbiology
dc.subject.mesh	Cell Cycle Proteins
dc.subject.mesh	Cell Division
dc.subject.mesh	Escherichia coli
dc.subject.mesh	Escherichia coli Proteins
dc.subject.mesh	Membrane Proteins
dc.subject.mesh	Mutation
dc.subject.mesh	Escherichia coli
dc.subject.mesh	Escherichia coli Proteins
dc.subject.mesh	Cell Cycle Proteins
dc.subject.mesh	Membrane Proteins
dc.subject.mesh	Cell Division
dc.subject.mesh	Mutation
dc.title	Coordinated disassembly of the divisome complex in Escherichia coli.
dc.type	Journal Article
utslib.citation.volume	101
utslib.location.activity	England
utslib.for	06 Biological Sciences
utslib.for	07 Agricultural and Veterinary Sciences
utslib.for	11 Medical and Health Sciences
pubs.organisational-group	/University of Technology Sydney
pubs.organisational-group	/University of Technology Sydney/Faculty of Science
pubs.organisational-group	/University of Technology Sydney/Strength - ithree - Institute of Infection, Immunity and Innovation
utslib.copyright.status	closed_access	*
dc.date.updated	2022-03-31T06:37:38Z
pubs.issue	3
pubs.publication-status	Published
pubs.volume	101
utslib.citation.issue	3

Abstract:

The divisome is the macromolecular complex that carries out cell division in Escherichia coli. Every generation it must be assembled, and then disassembled so that the sequestered proteins can be recycled. Whilst the assembly process has been well studied, virtually nothing is known about the disassembly process. In this study, we have used super-resolution SIM imaging to monitor pairs of fluorescently tagged divisome proteins as they depart from the division septum. These simple binary comparisons indicated that disassembly occurs in a coordinated process that consists of at least five steps: [FtsZ, ZapA] ⇒ [ZipA, FtsA] ⇒ [FtsL, FtsQ] ⇒ [FtsI, FtsN] ⇒ [FtsN]. This sequence of events is remarkably similar to the assembly process, indicating that disassembly follows a first-in, first-out principle. A secondary observation from these binary comparisons was that FtsZ and FtsN formed division rings that were spatially separated throughout the division process. Thus the data indicate that the divisome structure can be visualized as two concentric rings; a proto-ring containing FtsZ and an FtsN-ring.

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http://hdl.handle.net/10453/155794