A conserved cell division protein directly regulates FtsZ dynamics in filamentous and unicellular actinobacteria
Bacterial cell division is driven by the polymerization of the GTPase FtsZ into a contractile structure, the so-called Z-ring. This essential process involves proteins that modulate FtsZ dynamics and hence the overall Z-ring architecture. Actinobacteria like Streptomyces and Mycobacterium lack known...
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| Format: | Article |
| Language: | English |
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eLife Sciences Publications Ltd
2021-03-01
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| Series: | eLife |
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| Online Access: | https://elifesciences.org/articles/63387 |
| _version_ | 1811200290966208512 |
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| author | Félix Ramos-León Matthew J Bush Joseph W Sallmen Govind Chandra Jake Richardson Kim C Findlay Joseph R McCormick Susan Schlimpert |
| author_facet | Félix Ramos-León Matthew J Bush Joseph W Sallmen Govind Chandra Jake Richardson Kim C Findlay Joseph R McCormick Susan Schlimpert |
| author_sort | Félix Ramos-León |
| collection | DOAJ |
| description | Bacterial cell division is driven by the polymerization of the GTPase FtsZ into a contractile structure, the so-called Z-ring. This essential process involves proteins that modulate FtsZ dynamics and hence the overall Z-ring architecture. Actinobacteria like Streptomyces and Mycobacterium lack known key FtsZ-regulators. Here we report the identification of SepH, a conserved actinobacterial protein that directly regulates FtsZ dynamics. We show that SepH is crucially involved in cell division in Streptomyces venezuelae and that it binds FtsZ via a conserved helix-turn-helix motif, stimulating the assembly of FtsZ protofilaments. Comparative in vitro studies using the SepH homolog from Mycobacterium smegmatis further reveal that SepH can also bundle FtsZ protofilaments, indicating an additional Z-ring stabilizing function in vivo. We propose that SepH plays a crucial role at the onset of cytokinesis in actinobacteria by promoting the assembly of FtsZ filaments into division-competent Z-rings that can go on to mediate septum synthesis. |
| first_indexed | 2024-04-12T02:01:09Z |
| format | Article |
| id | doaj.art-4175039b4fe746c4840969c9a97470ea |
| institution | Directory Open Access Journal |
| issn | 2050-084X |
| language | English |
| last_indexed | 2024-04-12T02:01:09Z |
| publishDate | 2021-03-01 |
| publisher | eLife Sciences Publications Ltd |
| record_format | Article |
| series | eLife |
| spelling | doaj.art-4175039b4fe746c4840969c9a97470ea2022-12-22T03:52:39ZengeLife Sciences Publications LtdeLife2050-084X2021-03-011010.7554/eLife.63387A conserved cell division protein directly regulates FtsZ dynamics in filamentous and unicellular actinobacteriaFélix Ramos-León0Matthew J Bush1https://orcid.org/0000-0001-8216-0152Joseph W Sallmen2Govind Chandra3https://orcid.org/0000-0002-7882-6676Jake Richardson4Kim C Findlay5Joseph R McCormick6https://orcid.org/0000-0002-9071-7296Susan Schlimpert7https://orcid.org/0000-0001-6364-8056Department of Molecular Microbiology, John Innes Centre, Norwich, United KingdomDepartment of Molecular Microbiology, John Innes Centre, Norwich, United KingdomDepartment of Molecular Microbiology, John Innes Centre, Norwich, United KingdomDepartment of Molecular Microbiology, John Innes Centre, Norwich, United KingdomDepartment of Cell and Developmental Biology, John Innes Centre, Norwich, United KingdomDepartment of Cell and Developmental Biology, John Innes Centre, Norwich, United KingdomDepartment of Biological Sciences, Duquesne University, Pittsburgh, United StatesDepartment of Molecular Microbiology, John Innes Centre, Norwich, United KingdomBacterial cell division is driven by the polymerization of the GTPase FtsZ into a contractile structure, the so-called Z-ring. This essential process involves proteins that modulate FtsZ dynamics and hence the overall Z-ring architecture. Actinobacteria like Streptomyces and Mycobacterium lack known key FtsZ-regulators. Here we report the identification of SepH, a conserved actinobacterial protein that directly regulates FtsZ dynamics. We show that SepH is crucially involved in cell division in Streptomyces venezuelae and that it binds FtsZ via a conserved helix-turn-helix motif, stimulating the assembly of FtsZ protofilaments. Comparative in vitro studies using the SepH homolog from Mycobacterium smegmatis further reveal that SepH can also bundle FtsZ protofilaments, indicating an additional Z-ring stabilizing function in vivo. We propose that SepH plays a crucial role at the onset of cytokinesis in actinobacteria by promoting the assembly of FtsZ filaments into division-competent Z-rings that can go on to mediate septum synthesis.https://elifesciences.org/articles/63387Streptomyces venezuelaeMycobacterium smegmatisFtsZcell divisionsporulationprokaryotic development |
| spellingShingle | Félix Ramos-León Matthew J Bush Joseph W Sallmen Govind Chandra Jake Richardson Kim C Findlay Joseph R McCormick Susan Schlimpert A conserved cell division protein directly regulates FtsZ dynamics in filamentous and unicellular actinobacteria eLife Streptomyces venezuelae Mycobacterium smegmatis FtsZ cell division sporulation prokaryotic development |
| title | A conserved cell division protein directly regulates FtsZ dynamics in filamentous and unicellular actinobacteria |
| title_full | A conserved cell division protein directly regulates FtsZ dynamics in filamentous and unicellular actinobacteria |
| title_fullStr | A conserved cell division protein directly regulates FtsZ dynamics in filamentous and unicellular actinobacteria |
| title_full_unstemmed | A conserved cell division protein directly regulates FtsZ dynamics in filamentous and unicellular actinobacteria |
| title_short | A conserved cell division protein directly regulates FtsZ dynamics in filamentous and unicellular actinobacteria |
| title_sort | conserved cell division protein directly regulates ftsz dynamics in filamentous and unicellular actinobacteria |
| topic | Streptomyces venezuelae Mycobacterium smegmatis FtsZ cell division sporulation prokaryotic development |
| url | https://elifesciences.org/articles/63387 |
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