SepF is the FtsZ anchor in archaea, with features of an ancestral cell division system

Nika Pende, Adrià Sogues, Daniela Megrian, Anna Sartori-Rupp, Patrick England, Hayk Palabikyan, Simon K.-M. R. Rittmann, Martín Graña, Anne Marie Wehenkel (), Pedro M. Alzari and Simonetta Gribaldo ()
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Nika Pende: Evolutionary Biology of the Microbial Cell Unit, CNRS UMR2001, Department of Microbiology, Institut Pasteur
Adrià Sogues: Structural Microbiology Unit, Institut Pasteur, CNRS UMR 3528, Université de Paris
Daniela Megrian: Evolutionary Biology of the Microbial Cell Unit, CNRS UMR2001, Department of Microbiology, Institut Pasteur
Anna Sartori-Rupp: Ultrastructural BioImaging Unit, Institut Pasteur
Patrick England: Plate-forme de biophysique moléculaire, C2RT-Institut Pasteur, CNRS, UMR 3528
Hayk Palabikyan: Archaea Physiology & Biotechnology Group, Department of Functional and Evolutionary Ecology, University of Vienna
Simon K.-M. R. Rittmann: Archaea Physiology & Biotechnology Group, Department of Functional and Evolutionary Ecology, University of Vienna
Martín Graña: Bioinformatics Unit, Institut Pasteur of Montevideo
Anne Marie Wehenkel: Structural Microbiology Unit, Institut Pasteur, CNRS UMR 3528, Université de Paris
Pedro M. Alzari: Structural Microbiology Unit, Institut Pasteur, CNRS UMR 3528, Université de Paris
Simonetta Gribaldo: Evolutionary Biology of the Microbial Cell Unit, CNRS UMR2001, Department of Microbiology, Institut Pasteur

Nature Communications, 2021, vol. 12, issue 1, 1-13

Abstract: Abstract Most archaea divide by binary fission using an FtsZ-based system similar to that of bacteria, but they lack many of the divisome components described in model bacterial organisms. Notably, among the multiple factors that tether FtsZ to the membrane during bacterial cell constriction, archaea only possess SepF-like homologs. Here, we combine structural, cellular, and evolutionary analyses to demonstrate that SepF is the FtsZ anchor in the human-associated archaeon Methanobrevibacter smithii. 3D super-resolution microscopy and quantitative analysis of immunolabeled cells show that SepF transiently co-localizes with FtsZ at the septum and possibly primes the future division plane. M. smithii SepF binds to membranes and to FtsZ, inducing filament bundling. High-resolution crystal structures of archaeal SepF alone and in complex with the FtsZ C-terminal domain (FtsZCTD) reveal that SepF forms a dimer with a homodimerization interface driving a binding mode that is different from that previously reported in bacteria. Phylogenetic analyses of SepF and FtsZ from bacteria and archaea indicate that the two proteins may date back to the Last Universal Common Ancestor (LUCA), and we speculate that the archaeal mode of SepF/FtsZ interaction might reflect an ancestral feature. Our results provide insights into the mechanisms of archaeal cell division and pave the way for a better understanding of the processes underlying the divide between the two prokaryotic domains.

Date: 2021
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DOI: 10.1038/s41467-021-23099-8

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