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PomX, a ParA/MinD ATPase activating protein, is a triple regulator of cell division in Myxococcus xanthus
Cell division site positioning is precisely regulated but the underlying mechanisms are incompletely understood. In the social bacterium Myxococcus xanthus, the ~15 MDa tripartite PomX/Y/Z complex associates with and translocates across the nucleoid in a PomZ ATPase-dependent manner to directly posi...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
eLife Sciences Publications, Ltd
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7993993/ https://www.ncbi.nlm.nih.gov/pubmed/33734087 http://dx.doi.org/10.7554/eLife.66160 |
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author | Schumacher, Dominik Harms, Andrea Bergeler, Silke Frey, Erwin Søgaard-Andersen, Lotte |
author_facet | Schumacher, Dominik Harms, Andrea Bergeler, Silke Frey, Erwin Søgaard-Andersen, Lotte |
author_sort | Schumacher, Dominik |
collection | PubMed |
description | Cell division site positioning is precisely regulated but the underlying mechanisms are incompletely understood. In the social bacterium Myxococcus xanthus, the ~15 MDa tripartite PomX/Y/Z complex associates with and translocates across the nucleoid in a PomZ ATPase-dependent manner to directly position and stimulate formation of the cytokinetic FtsZ-ring at midcell, and then undergoes fission during division. Here, we demonstrate that PomX consists of two functionally distinct domains and has three functions. The N-terminal domain stimulates ATPase activity of the ParA/MinD ATPase PomZ. The C-terminal domain interacts with PomY and forms polymers, which serve as a scaffold for PomX/Y/Z complex formation. Moreover, the PomX/PomZ interaction is important for fission of the PomX/Y/Z complex. These observations together with previous work support that the architecturally diverse ATPase activating proteins of ParA/MinD ATPases are highly modular and use the same mechanism to activate their cognate ATPase via a short positively charged N-terminal extension. |
format | Online Article Text |
id | pubmed-7993993 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | eLife Sciences Publications, Ltd |
record_format | MEDLINE/PubMed |
spelling | pubmed-79939932021-03-26 PomX, a ParA/MinD ATPase activating protein, is a triple regulator of cell division in Myxococcus xanthus Schumacher, Dominik Harms, Andrea Bergeler, Silke Frey, Erwin Søgaard-Andersen, Lotte eLife Cell Biology Cell division site positioning is precisely regulated but the underlying mechanisms are incompletely understood. In the social bacterium Myxococcus xanthus, the ~15 MDa tripartite PomX/Y/Z complex associates with and translocates across the nucleoid in a PomZ ATPase-dependent manner to directly position and stimulate formation of the cytokinetic FtsZ-ring at midcell, and then undergoes fission during division. Here, we demonstrate that PomX consists of two functionally distinct domains and has three functions. The N-terminal domain stimulates ATPase activity of the ParA/MinD ATPase PomZ. The C-terminal domain interacts with PomY and forms polymers, which serve as a scaffold for PomX/Y/Z complex formation. Moreover, the PomX/PomZ interaction is important for fission of the PomX/Y/Z complex. These observations together with previous work support that the architecturally diverse ATPase activating proteins of ParA/MinD ATPases are highly modular and use the same mechanism to activate their cognate ATPase via a short positively charged N-terminal extension. eLife Sciences Publications, Ltd 2021-03-18 /pmc/articles/PMC7993993/ /pubmed/33734087 http://dx.doi.org/10.7554/eLife.66160 Text en © 2021, Schumacher et al http://creativecommons.org/licenses/by/4.0/ http://creativecommons.org/licenses/by/4.0/This article is distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use and redistribution provided that the original author and source are credited. |
spellingShingle | Cell Biology Schumacher, Dominik Harms, Andrea Bergeler, Silke Frey, Erwin Søgaard-Andersen, Lotte PomX, a ParA/MinD ATPase activating protein, is a triple regulator of cell division in Myxococcus xanthus |
title | PomX, a ParA/MinD ATPase activating protein, is a triple regulator of cell division in Myxococcus xanthus |
title_full | PomX, a ParA/MinD ATPase activating protein, is a triple regulator of cell division in Myxococcus xanthus |
title_fullStr | PomX, a ParA/MinD ATPase activating protein, is a triple regulator of cell division in Myxococcus xanthus |
title_full_unstemmed | PomX, a ParA/MinD ATPase activating protein, is a triple regulator of cell division in Myxococcus xanthus |
title_short | PomX, a ParA/MinD ATPase activating protein, is a triple regulator of cell division in Myxococcus xanthus |
title_sort | pomx, a para/mind atpase activating protein, is a triple regulator of cell division in myxococcus xanthus |
topic | Cell Biology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7993993/ https://www.ncbi.nlm.nih.gov/pubmed/33734087 http://dx.doi.org/10.7554/eLife.66160 |
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