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- Publisher Website: 10.1038/ncomms6341
- Scopus: eid_2-s2.0-84921715486
- WOS: WOS:000347220300002
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Article: MinCD cell division proteins form alternating copolymeric cytomotive filaments
Title | MinCD cell division proteins form alternating copolymeric cytomotive filaments |
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Authors | |
Issue Date | 2014 |
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 Identifier | http://hdl.handle.net/10722/219384 |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Ghosal, Debnath | - |
dc.contributor.author | Trambaiolo, Daniel | - |
dc.contributor.author | Amos, Linda A. | - |
dc.contributor.author | Lowe, Jan | - |
dc.date.accessioned | 2015-09-23T02:56:56Z | - |
dc.date.available | 2015-09-23T02:56:56Z | - |
dc.date.issued | 2014 | - |
dc.identifier.citation | Nature Communications, 2014, v. 5 | - |
dc.identifier.uri | http://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.language | eng | - |
dc.relation.ispartof | Nature Communications | - |
dc.title | MinCD cell division proteins form alternating copolymeric cytomotive filaments | - |
dc.type | Article | - |
dc.description.nature | link_to_OA_fulltext | - |
dc.identifier.doi | 10.1038/ncomms6341 | - |
dc.identifier.scopus | eid_2-s2.0-84921715486 | - |
dc.identifier.volume | 5 | - |
dc.identifier.eissn | 2041-1723 | - |
dc.identifier.isi | WOS:000347220300002 | - |
dc.identifier.f1000 | 725276378 | - |
dc.identifier.issnl | 2041-1723 | - |