The speed of FtsZ treadmilling is tightly regulated by membrane binding
Abstract As one of the key elements in bacterial cell division, the cytoskeletal protein FtsZ appears to be highly involved in circumferential treadmilling along the inner membrane, yielding circular vortices when transferred to flat membranes. However, it remains unclear how a membrane-targeted pro...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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Nature Portfolio
2020-06-01
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| Series: | Scientific Reports |
| Online Access: | https://doi.org/10.1038/s41598-020-67224-x |
| _version_ | 1830084814680621056 |
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| author | Daniela A. García-Soriano Tamara Heermann Ana Raso Germán Rivas Petra Schwille |
| author_facet | Daniela A. García-Soriano Tamara Heermann Ana Raso Germán Rivas Petra Schwille |
| author_sort | Daniela A. García-Soriano |
| collection | DOAJ |
| description | Abstract As one of the key elements in bacterial cell division, the cytoskeletal protein FtsZ appears to be highly involved in circumferential treadmilling along the inner membrane, yielding circular vortices when transferred to flat membranes. However, it remains unclear how a membrane-targeted protein can produce these dynamics. Here, we dissect the roles of membrane binding, GTPase activity, and the unstructured C-terminal linker on the treadmilling of a chimera FtsZ protein through in vitro reconstitution of different FtsZ-YFP-mts variants on supported membranes. In summary, our results suggest substantial robustness of dynamic vortex formation, where only significant mutations, resulting in abolished membrane binding or compromised lateral interactions, are detrimental for the generation of treadmilling rings. In addition to GTPase activity, which directly affects treadmilling dynamics, we found a striking correlation of membrane binding with treadmilling speed as a result of changing the MTS on our chimera proteins. This discovery leads to the hypothesis that the in vivo existence of two alternative tether proteins for FtsZ could be a mechanism for controlling FtsZ treadmilling. |
| first_indexed | 2024-12-14T16:49:21Z |
| format | Article |
| id | doaj.art-8abeee3857ef495c848283c51c99a60d |
| institution | Directory Open Access Journal |
| issn | 2045-2322 |
| language | English |
| last_indexed | 2024-12-14T16:49:21Z |
| publishDate | 2020-06-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Scientific Reports |
| spelling | doaj.art-8abeee3857ef495c848283c51c99a60d2022-12-21T22:54:06ZengNature PortfolioScientific Reports2045-23222020-06-011011910.1038/s41598-020-67224-xThe speed of FtsZ treadmilling is tightly regulated by membrane bindingDaniela A. García-Soriano0Tamara Heermann1Ana Raso2Germán Rivas3Petra Schwille4Department of Cellular and Molecular Biophysics, Max Planck Institute for Biochemistry, MartinsriedDepartment of Cellular and Molecular Biophysics, Max Planck Institute for Biochemistry, MartinsriedDepartment of Cellular and Molecular Biophysics, Max Planck Institute for Biochemistry, MartinsriedCentro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas (CSIC)Department of Cellular and Molecular Biophysics, Max Planck Institute for Biochemistry, MartinsriedAbstract As one of the key elements in bacterial cell division, the cytoskeletal protein FtsZ appears to be highly involved in circumferential treadmilling along the inner membrane, yielding circular vortices when transferred to flat membranes. However, it remains unclear how a membrane-targeted protein can produce these dynamics. Here, we dissect the roles of membrane binding, GTPase activity, and the unstructured C-terminal linker on the treadmilling of a chimera FtsZ protein through in vitro reconstitution of different FtsZ-YFP-mts variants on supported membranes. In summary, our results suggest substantial robustness of dynamic vortex formation, where only significant mutations, resulting in abolished membrane binding or compromised lateral interactions, are detrimental for the generation of treadmilling rings. In addition to GTPase activity, which directly affects treadmilling dynamics, we found a striking correlation of membrane binding with treadmilling speed as a result of changing the MTS on our chimera proteins. This discovery leads to the hypothesis that the in vivo existence of two alternative tether proteins for FtsZ could be a mechanism for controlling FtsZ treadmilling.https://doi.org/10.1038/s41598-020-67224-x |
| spellingShingle | Daniela A. García-Soriano Tamara Heermann Ana Raso Germán Rivas Petra Schwille The speed of FtsZ treadmilling is tightly regulated by membrane binding Scientific Reports |
| title | The speed of FtsZ treadmilling is tightly regulated by membrane binding |
| title_full | The speed of FtsZ treadmilling is tightly regulated by membrane binding |
| title_fullStr | The speed of FtsZ treadmilling is tightly regulated by membrane binding |
| title_full_unstemmed | The speed of FtsZ treadmilling is tightly regulated by membrane binding |
| title_short | The speed of FtsZ treadmilling is tightly regulated by membrane binding |
| title_sort | speed of ftsz treadmilling is tightly regulated by membrane binding |
| url | https://doi.org/10.1038/s41598-020-67224-x |
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