Architecture of the ring formed by the tubulin homologue FtsZ in bacterial cell division
Membrane constriction is a prerequisite for cell division. The most common membrane constriction system in prokaryotes is based on the tubulin homologue FtsZ, whose filaments in E. coli are anchored to the membrane by FtsA and enable the formation of the Z-ring and divisome. The precise architecture...
| Main Authors: | , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
eLife Sciences Publications Ltd
2014-12-01
|
| Series: | eLife |
| Subjects: | |
| Online Access: | https://elifesciences.org/articles/04601 |
| _version_ | 1811180633557303296 |
|---|---|
| author | Piotr Szwedziak Qing Wang Tanmay A M Bharat Matthew Tsim Jan Löwe |
| author_facet | Piotr Szwedziak Qing Wang Tanmay A M Bharat Matthew Tsim Jan Löwe |
| author_sort | Piotr Szwedziak |
| collection | DOAJ |
| description | Membrane constriction is a prerequisite for cell division. The most common membrane constriction system in prokaryotes is based on the tubulin homologue FtsZ, whose filaments in E. coli are anchored to the membrane by FtsA and enable the formation of the Z-ring and divisome. The precise architecture of the FtsZ ring has remained enigmatic. In this study, we report three-dimensional arrangements of FtsZ and FtsA filaments in C. crescentus and E. coli cells and inside constricting liposomes by means of electron cryomicroscopy and cryotomography. In vivo and in vitro, the Z-ring is composed of a small, single-layered band of filaments parallel to the membrane, creating a continuous ring through lateral filament contacts. Visualisation of the in vitro reconstituted constrictions as well as a complete tracing of the helical paths of the filaments with a molecular model favour a mechanism of FtsZ-based membrane constriction that is likely to be accompanied by filament sliding. |
| first_indexed | 2024-04-11T09:06:27Z |
| format | Article |
| id | doaj.art-acf83977e7734dda9d930d013f4894f4 |
| institution | Directory Open Access Journal |
| issn | 2050-084X |
| language | English |
| last_indexed | 2024-04-11T09:06:27Z |
| publishDate | 2014-12-01 |
| publisher | eLife Sciences Publications Ltd |
| record_format | Article |
| series | eLife |
| spelling | doaj.art-acf83977e7734dda9d930d013f4894f42022-12-22T04:32:37ZengeLife Sciences Publications LtdeLife2050-084X2014-12-01310.7554/eLife.04601Architecture of the ring formed by the tubulin homologue FtsZ in bacterial cell divisionPiotr Szwedziak0https://orcid.org/0000-0002-5766-0873Qing Wang1Tanmay A M Bharat2Matthew Tsim3Jan Löwe4Structural Studies Division, MRC Laboratory of Molecular Biology, Cambridge, United KingdomStructural Studies Division, MRC Laboratory of Molecular Biology, Cambridge, United KingdomStructural Studies Division, MRC Laboratory of Molecular Biology, Cambridge, United KingdomStructural Studies Division, MRC Laboratory of Molecular Biology, Cambridge, United KingdomStructural Studies Division, MRC Laboratory of Molecular Biology, Cambridge, United KingdomMembrane constriction is a prerequisite for cell division. The most common membrane constriction system in prokaryotes is based on the tubulin homologue FtsZ, whose filaments in E. coli are anchored to the membrane by FtsA and enable the formation of the Z-ring and divisome. The precise architecture of the FtsZ ring has remained enigmatic. In this study, we report three-dimensional arrangements of FtsZ and FtsA filaments in C. crescentus and E. coli cells and inside constricting liposomes by means of electron cryomicroscopy and cryotomography. In vivo and in vitro, the Z-ring is composed of a small, single-layered band of filaments parallel to the membrane, creating a continuous ring through lateral filament contacts. Visualisation of the in vitro reconstituted constrictions as well as a complete tracing of the helical paths of the filaments with a molecular model favour a mechanism of FtsZ-based membrane constriction that is likely to be accompanied by filament sliding.https://elifesciences.org/articles/04601bacterial cytoskeletoncytokinesiscell divisionC. crescentusFtsZelectron tomography |
| spellingShingle | Piotr Szwedziak Qing Wang Tanmay A M Bharat Matthew Tsim Jan Löwe Architecture of the ring formed by the tubulin homologue FtsZ in bacterial cell division eLife bacterial cytoskeleton cytokinesis cell division C. crescentus FtsZ electron tomography |
| title | Architecture of the ring formed by the tubulin homologue FtsZ in bacterial cell division |
| title_full | Architecture of the ring formed by the tubulin homologue FtsZ in bacterial cell division |
| title_fullStr | Architecture of the ring formed by the tubulin homologue FtsZ in bacterial cell division |
| title_full_unstemmed | Architecture of the ring formed by the tubulin homologue FtsZ in bacterial cell division |
| title_short | Architecture of the ring formed by the tubulin homologue FtsZ in bacterial cell division |
| title_sort | architecture of the ring formed by the tubulin homologue ftsz in bacterial cell division |
| topic | bacterial cytoskeleton cytokinesis cell division C. crescentus FtsZ electron tomography |
| url | https://elifesciences.org/articles/04601 |
| work_keys_str_mv | AT piotrszwedziak architectureoftheringformedbythetubulinhomologueftszinbacterialcelldivision AT qingwang architectureoftheringformedbythetubulinhomologueftszinbacterialcelldivision AT tanmayambharat architectureoftheringformedbythetubulinhomologueftszinbacterialcelldivision AT matthewtsim architectureoftheringformedbythetubulinhomologueftszinbacterialcelldivision AT janlowe architectureoftheringformedbythetubulinhomologueftszinbacterialcelldivision |