An ATP-dependent partner switch links flagellar C-ring assembly with gene expression
- Blagotinsek, Vitan Center for Synthetic Microbiology (SYNMIKRO), Philipps-University Marburg, 35043 Marburg, Germany - Department of Chemistry, Philipps-University Marburg, 35043 Marburg, Germany
- Schwan, Meike Department of Microbiology and Molecular Biology, Justus-Liebig-Universität, 35392 Giessen, Germany
- Steinchen, Wieland Center for Synthetic Microbiology (SYNMIKRO), Philipps-University Marburg, 35043 Marburg, Germany - Department of Chemistry, Philipps-University Marburg, 35043 Marburg, Germany
- Mrusek, Devid Center for Synthetic Microbiology (SYNMIKRO), Philipps-University Marburg, 35043 Marburg, Germany - Department of Chemistry, Philipps-University Marburg, 35043 Marburg, Germany
- Hook, John C. Department of Microbiology and Molecular Biology, Justus-Liebig-Universität, 35392 Giessen, Germany
- Rossmann, Florian Department of Microbiology and Molecular Biology, Justus-Liebig-Universität, 35392 Giessen, Germany - Department of Life Sciences, Imperial College London, London SW7 2AZ, United Kingdom
- Freibert, Sven A. Institut für Zytobiologie und Zytopathologie, Philipps-Universität Marburg, 35032 Marburg, Germany
- Kratzat, Hanna Genzentrum, Ludwig-Maximilians-Universität, 81377 Munich, Germany - Department of Biochemistry, Ludwig-Maximilians-Universität, 81377 Munich, Germany
- Murat, Guillaume Department of Biology, University of Fribourg, 1700 Fribourg, Switzerland
- Kressler, Dieter Department of Biology, University of Fribourg, 1700 Fribourg, Switzerland
- Beckmann, Roland Genzentrum, Ludwig-Maximilians-Universität, 81377 Munich, Germany - Department of Biochemistry, Ludwig-Maximilians-Universität, 81377 Munich, Germany
- Beeby, Morgan Department of Life Sciences, Imperial College London, London SW7 2AZ, United Kingdom
- Thormann, Kai M. Department of Microbiology and Molecular Biology, Justus-Liebig-Universität, 35392 Giessen, Germany
- Bange, Gert Center for Synthetic Microbiology (SYNMIKRO), Philipps-University Marburg, 35043 Marburg, Germany - Department of Chemistry, Philipps-University Marburg, 35043 Marburg, Germany
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25.08.2020
Published in:
- Proceedings of the National Academy of Sciences. - 2020, vol. 117, no. 34, p. 20826–20835
English
Bacterial flagella differ in their number and spatial arrangement. In many species, the MinD-type ATPase FlhG (also YlxH/FleN) is central to the numerical control of bacterial flagella, and its deletion in polarly flagellated bacteria typically leads to hyperflagellation. The molecular mechanism underlying this numerical control, however, remains enigmatic. Using the model species Shewanella putrefaciens, we show that FlhG links assembly of the flagellar C ring with the action of the master transcriptional regulator FlrA (named FleQ in other species). While FlrA and the flagellar C-ring protein FliM have an overlapping binding site on FlhG, their binding depends on the ATP-dependent dimerization state of FlhG. FliM interacts with FlhG independent of nucleotide binding, while FlrA exclusively interacts with the ATP- dependent FlhG dimer and stimulates FlhG ATPase activity. Our in vivo analysis of FlhG partner switching between FliM and FlrA reveals its mechanism in the numerical restriction of flagella, in which the transcriptional activity of FlrA is down-regulated through a negative feedback loop. Our study demonstrates another level of regulatory complexity underlying the spationumerical regulation of flagellar biogenesis and implies that flagellar assembly transcriptionally regulates the production of more initial building blocks.
- Faculty
- Faculté des sciences et de médecine
- Department
- Département de Biologie
- Language
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- English
- Classification
- Biological sciences
- License
- License undefined
- Identifiers
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- RERO DOC 329616
- DOI 10.1073/pnas.2006470117
- Persistent URL
- https://folia.unifr.ch/unifr/documents/309059
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