Essential dynamic interdependence of FtsZ and SepF for Z-ring and septum formation in Corynebacterium glutamicum
In: Nature Communications, Jg. 11 (2020), Heft 1, S. 1-14
Online
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Zugriff:
The mechanisms of Z-ring assembly and regulation in bacteria are poorly understood, particularly in non-model organisms. Actinobacteria, a large bacterial phylum that includes the pathogen Mycobacterium tuberculosis, lack the canonical FtsZ-membrane anchors and Z-ring regulators described for E. coli. Here we investigate the physiological function of Corynebacterium glutamicum SepF, the only cell division-associated protein from Actinobacteria known to interact with the conserved C-terminal tail of FtsZ. We show an essential interdependence of FtsZ and SepF for formation of a functional Z-ring in C. glutamicum. The crystal structure of the SepF–FtsZ complex reveals a hydrophobic FtsZ-binding pocket, which defines the SepF homodimer as the functional unit, and suggests a reversible oligomerization interface. FtsZ filaments and lipid membranes have opposing effects on SepF polymerization, indicating that SepF has multiple roles at the cell division site, involving FtsZ bundling, Z-ring tethering and membrane reshaping activities that are needed for proper Z-ring assembly and function.
The mechanisms of Z-ring assembly and regulation in bacteria are poorly understood, particularly in non-model organisms. Here, Sogues et al. study the interaction between FtsZ and SepF in Corynebacterium glutamicum, showing an essential interdependence of these proteins for formation of a functional Z-ring.
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Essential dynamic interdependence of FtsZ and SepF for Z-ring and septum formation in Corynebacterium glutamicum
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| Autor/in / Beteiligte Person: | Gaday, Quentin ; Anne Marie Wehenkel ; Sogues, Adrià ; Trépout, Sylvain ; Durán, Rosario ; Chenal, Alexandre ; Mathilde Ben Assaya ; Graña, Martín ; Alzari, Pedro M. ; Martinez, Mariano A. ; Voegele, Alexis ; England, Patrick ; Haouz, Ahmed ; VanNieuwenhze, Michael S. ; Microbiologie structurale - Structural Microbiology (Microb. Struc. (UMR_3528 / U-Pasteur_5)) ; Institut Pasteur [Paris] (IP)-Université Paris Diderot - Paris 7 (UPD7)-Centre National de la Recherche Scientifique (CNRS) ; Bioinformatics / Bioinformática [Montevideo] ; Institut Pasteur de Montevideo ; Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP) ; Biochimie des Interactions Macromoléculaires / Biochemistry of Macromolecular Interactions ; Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS) ; Department of Chemistry, Indiana University ; Indiana University [Bloomington] ; Indiana University System-Indiana University System ; Biophysique Moléculaire (Plate-forme) ; Cristallographie (Plateforme) - Crystallography (Platform) ; Institut Curie [Paris] ; Chimie et modélisation pour la biologie du cancer (CMBC) ; Institut Curie [Paris]-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut de Chimie du CNRS (INC)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS) ; Analytical Biochemistry and Proteomics / Bioquímica y Proteómica Analíticas [Montevideo] ; This work was partially supported by grants from the Institut Pasteur (Paris), the CNRS (France) and the Agence Nationale de la Recherche (PhoCellDiv, ANR-18-CE11-0017-01). A.S. is part of the Pasteur-Paris University (PPU) International Ph.D Program, funded by the European Union’s Horizon 2020 research and innovation program under the Marie Sklodowska-Curie grant agreement No 665807. Q.G. was funded by MTCI Ph.D school (ED 563) ; A.V. was supported by a DIM MalInf (infectious diseases) grant. M.G. acknowledges support from Programa de Desarrollo de las Ciencias Básicas and Sistema Nacional de Investigación e Innovación, Uruguay. ; We thank A. Ducret for help with MicrobeJ, F. Gubellini for help with electron microscopy, M. Bott and M. Baumgart for the pk19-P3323-lcpA plasmid and help with corynebacterial genetics, and H. Gramajo for the pTGR5 plasmid. We gratefully acknowledge the core facilities at the Institut Pasteur C2RT, in particular G. Pehau-Arnaudet (UBI), B. Raynal, S. Brule (PFBMI), P. Weber, C. Pissis (PFC), and J. Fernandes (UtechS PBI/Imagopole, supported by France BioImaging ; ANR-10–INSB–04 ; Investments for the Future). We thank the staff of ESRF and of EMBL-Grenoble for assistance and support in using beamlines ID30B and ID23-1, and the staff of SOLEIL Synchrotron for assistance in using the beamline Disco. We acknowledge the PICT-IBISA for providing access to the cryo-EM facility at Orsay. Finally, we would like to thank the reviewers for their coments and suggestions, which have helped us to improve the quality of the manuscript. ; ANR-18-CE11-0017,PhoCellDiv,Mécanismes moléculaires phospho-dépendants de l'assemblage et de la régulation du divisome bactérien(2018) ; European Project: 665807,H2020,H2020-MSCA-COFUND-2014,PASTEURDOC(2015) ; BENEDIC, Bénédicte ; APPEL À PROJETS GÉNÉRIQUE 2018 - Mécanismes moléculaires phospho-dépendants de l'assemblage et de la régulation du divisome bactérien - - PhoCellDiv2018 - ANR-18-CE11-0017 - AAPG2018 -, VALID ; Institut Pasteur International Docotal Program - PASTEURDOC - - H20202015-10-01 - 2020-10-01 - 665807 -, VALID ; Institut Pasteur [Paris]-Université Paris Diderot - Paris 7 (UPD7)-Centre National de la Recherche Scientifique (CNRS) ; Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS) ; Université Paris Diderot - Paris 7 (UPD7)-Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS) |
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| Zeitschrift: | Nature Communications, Jg. 11 (2020), Heft 1, S. 1-14 |
| Veröffentlichung: | Nature Publishing Group, 2020 |
| Medientyp: | unknown |
| ISSN: | 2041-1723 (print) |
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