Two FtsZ proteins orchestrate archaeal cell division through distinct functions in ring assembly and constriction

Liao, Y; Ithurbide, S; Löwe, J; Duggin, IG

Two FtsZ proteins orchestrate archaeal cell division through distinct functions in ring assembly and constriction

Liao, Y

Ithurbide, S

Löwe, J Duggin, IG

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Publisher:: Cold Spring Harbor Laboratory
Publication Type:: Journal Article
Citation:: BioRxiv, 2022, pp. 2020.06.04.133736
Issue Date:: 2022-01-01

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Field	Value	Language
dc.contributor.author	Liao, Y https://orcid.org/0000-0002-8492-2648
dc.contributor.author	Ithurbide, S https://orcid.org/0000-0002-1533-8472
dc.contributor.author	Löwe, J
dc.contributor.author	Duggin, IG
dc.date.accessioned	2022-03-25T05:56:38Z
dc.date.available	2022-03-25T05:56:38Z
dc.date.issued	2022-01-01
dc.identifier.citation	BioRxiv, 2022, pp. 2020.06.04.133736
dc.identifier.uri	http://hdl.handle.net/10453/155582
dc.description.abstract	<jats:title>Abstract</jats:title><jats:p>The tubulin homolog FtsZ assembles a ring in bacteria and plays a key role in the machinery that constricts to divide the cells. Many archaea encode two FtsZs from distinct families, FtsZ1 and FtsZ2, of previously unclear functions. We show that <jats:italic>Haloferax volcanii</jats:italic> cannot divide properly without either or both but proliferates in alternative ways via remarkable envelope plasticity. The FtsZs co-localize as a dynamic midcell division ring. FtsZ1 independently assembles and stabilizes FtsZ2 in the ring, and influences cell shape, whereas FtsZ2 functions in the constriction mechanism; their GTPase active sites are crucial for these activities. The two FtsZs are widespread in archaea with a single S-layer envelope, but those with a pseudomurein wall only have FtsZ1. FtsZ2 appears to be essential for constriction of the flexible membrane-S-layer, where an internal constriction force might dominate the division mechanism in contrast to bacteria and archaea that divide by wall ingrowth.</jats:p>
dc.language	en
dc.publisher	Cold Spring Harbor Laboratory
dc.relation	http://purl.org/au-research/grants/arc/FT160100010
dc.relation.ispartof	BioRxiv
dc.relation.isbasedon	10.1101/2020.06.04.133736
dc.rights	info:eu-repo/semantics/openAccess
dc.rights	This is a post-peer-review, pre-copyedit version of an article published in [Nat Microbiol. 2021 May 01; 6(5): 594–605.]. The final authenticated version is available online at: http://dx.doi.org/[doi:10.1038/s41564-021-00894-z]”
dc.title	Two FtsZ proteins orchestrate archaeal cell division through distinct functions in ring assembly and constriction
dc.type	Journal Article
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	open_access	*
pubs.consider-herdc	true
dc.date.updated	2022-03-25T05:56:34Z
pubs.publication-status	In preparation

Abstract:

AbstractThe tubulin homolog FtsZ assembles a ring in bacteria and plays a key role in the machinery that constricts to divide the cells. Many archaea encode two FtsZs from distinct families, FtsZ1 and FtsZ2, of previously unclear functions. We show that Haloferax volcanii cannot divide properly without either or both but proliferates in alternative ways via remarkable envelope plasticity. The FtsZs co-localize as a dynamic midcell division ring. FtsZ1 independently assembles and stabilizes FtsZ2 in the ring, and influences cell shape, whereas FtsZ2 functions in the constriction mechanism; their GTPase active sites are crucial for these activities. The two FtsZs are widespread in archaea with a single S-layer envelope, but those with a pseudomurein wall only have FtsZ1. FtsZ2 appears to be essential for constriction of the flexible membrane-S-layer, where an internal constriction force might dominate the division mechanism in contrast to bacteria and archaea that divide by wall ingrowth.

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http://hdl.handle.net/10453/155582