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Article: MinCD cell division proteins form alternating copolymeric cytomotive filaments

TitleMinCD cell division proteins form alternating copolymeric cytomotive filaments
Authors
Issue Date2014
Citation
Nature Communications, 2014, v. 5 How to Cite?
Abstract© 2014 Macmillan Publishers Limited. During bacterial cell division, filaments of the tubulin-like protein FtsZ assemble at midcell to form the cytokinetic Z-ring. Its positioning is regulated by the oscillation of MinCDE proteins. MinC is activated by MinD through an unknown mechanism and prevents Z-ring assembly anywhere but midcell. Here, using X-ray crystallography, electron microscopy and in vivo analyses, we show that MinD activates MinC by forming a new class of alternating copolymeric filaments that show similarity to eukaryotic septin filaments. A non-polymerizing mutation in MinD causes aberrant cell division in Escherichia coli. MinCD copolymers bind to membrane, interact with FtsZ and are disassembled by MinE. Imaging a functional msfGFP-MinC fusion protein in MinE-deleted cells reveals filamentous structures. EM imaging of our reconstitution of the MinCD-FtsZ interaction on liposome surfaces reveals a plausible mechanism for regulation of FtsZ ring assembly by MinCD copolymers.
Persistent Identifierhttp://hdl.handle.net/10722/219384

 

DC FieldValueLanguage
dc.contributor.authorGhosal, Debnath-
dc.contributor.authorTrambaiolo, Daniel-
dc.contributor.authorAmos, Linda A.-
dc.contributor.authorLowe, Jan-
dc.date.accessioned2015-09-23T02:56:56Z-
dc.date.available2015-09-23T02:56:56Z-
dc.date.issued2014-
dc.identifier.citationNature Communications, 2014, v. 5-
dc.identifier.urihttp://hdl.handle.net/10722/219384-
dc.description.abstract© 2014 Macmillan Publishers Limited. During bacterial cell division, filaments of the tubulin-like protein FtsZ assemble at midcell to form the cytokinetic Z-ring. Its positioning is regulated by the oscillation of MinCDE proteins. MinC is activated by MinD through an unknown mechanism and prevents Z-ring assembly anywhere but midcell. Here, using X-ray crystallography, electron microscopy and in vivo analyses, we show that MinD activates MinC by forming a new class of alternating copolymeric filaments that show similarity to eukaryotic septin filaments. A non-polymerizing mutation in MinD causes aberrant cell division in Escherichia coli. MinCD copolymers bind to membrane, interact with FtsZ and are disassembled by MinE. Imaging a functional msfGFP-MinC fusion protein in MinE-deleted cells reveals filamentous structures. EM imaging of our reconstitution of the MinCD-FtsZ interaction on liposome surfaces reveals a plausible mechanism for regulation of FtsZ ring assembly by MinCD copolymers.-
dc.languageeng-
dc.relation.ispartofNature Communications-
dc.titleMinCD cell division proteins form alternating copolymeric cytomotive filaments-
dc.typeArticle-
dc.description.natureLink_to_subscribed_fulltext-
dc.identifier.doi10.1038/ncomms6341-
dc.identifier.scopuseid_2-s2.0-84921715486-
dc.identifier.volume5-
dc.identifier.eissn2041-1723-
dc.identifier.f1000725276378-

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