Distinct filament morphology and membrane tethering features of the dual FtsZ paralogs in Odinarchaeota

The Asgard phylum has emerged as a model to study eukaryogenesis because of their close relatedness with the eukaryotes. In this study, we use FtsZ proteins from a member of the class Odinarchaeia as representatives to investigate the probable origin, evolution, and assembly of the FtsZ/tubulin protein superfamily in Asgard archaea. We performed a comparative analysis of the biochemical properties and cytoskeletal assembly of FtsZ1 and FtsZ2, the two FtsZ isoforms in the Odinarchaeota metagenome. Our electron microscopy analysis reveals that OdinFtsZ1 assembles into curved single protofilaments, while OdinFtsZ2 forms stacked spiral ring-like structures. Upon sequence analysis, we identified an N-terminal amphipathic helix in OdinFtsZ1, which mediates direct membrane tethering. In contrast, OdinFtsZ2 is recruited to the membrane by the anchor OdinSepF via OdinFtsZ2's C-terminal tail. Overall, we report the presence of two distant evolutionary paralogs of FtsZ in Odinarchaeota, with distinct filament assemblies and differing modes of membrane targeting. Our findings highlight the diversity of FtsZ proteins in the archaeal phylum Asgardarchaeota, providing valuable insights into the evolution and differentiation of tubulin-family proteins.

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Publication Details

Journal
The EMBO Journal
Published
2025-08-08
DOI
https://doi.org/10.1038/s44318-025-00529-7
Primary Topic
Genomics and Phylogenetic Studies
Type
article
Field-Weighted Citation Impact
0.00

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article

Distinct filament morphology and membrane tethering features of the dual FtsZ paralogs in Odinarchaeota

Srijita Roy, Soumyajit Dutta, Jayanti Kumari, Abhishek Dhar et al.
The EMBO Journal
Genomics and Phylogenetic Studies
article

Distinct filament morphology and membrane tethering features of the dual FtsZ paralogs in Odinarchaeota

Srijita Roy, Soumyajit Dutta, Jayanti Kumari, Abhishek Dhar, Animesh Kundu, Samay Pande, Saravanan Palani, R. Srinivasan, Vaibhav Sharma, Pananghat Gayathri, Kutti R. Vinothkumar, Sucharita Bose, Akhilesh Uthaman
article en

Abstract

The Asgard phylum has emerged as a model to study eukaryogenesis because of their close relatedness with the eukaryotes. In this study, we use FtsZ proteins from a member of the class Odinarchaeia as representatives to investigate the probable origin, evolution, and assembly of the FtsZ/tubulin protein superfamily in Asgard archaea. We performed a comparative analysis of the biochemical properties and cytoskeletal assembly of FtsZ1 and FtsZ2, the two FtsZ isoforms in the Odinarchaeota metagenome. Our electron microscopy analysis reveals that OdinFtsZ1 assembles into curved single protofilaments, while OdinFtsZ2 forms stacked spiral ring-like structures. Upon sequence analysis, we identified an N-terminal amphipathic helix in OdinFtsZ1, which mediates direct membrane tethering. In contrast, OdinFtsZ2 is recruited to the membrane by the anchor OdinSepF via OdinFtsZ2's C-terminal tail. Overall, we report the presence of two distant evolutionary paralogs of FtsZ in Odinarchaeota, with distinct filament assemblies and differing modes of membrane targeting. Our findings highlight the diversity of FtsZ proteins in the archaeal phylum Asgardarchaeota, providing valuable insights into the evolution and differentiation of tubulin-family proteins.

The EMBO JournalVol. 44(21)
National Institute of Science Education and Research (IN), Indian Institute of Science Education and Research Pune (IN), National Centre for Biological Sciences (IN), Homi Bhabha National Institute (IN), Institute for Stem Cell Biology and Regenerative Medicine (IN), Indian Institute of Science Bangalore (IN), Amrita Vishwa Vidyapeetham (IN)
Department of Biotechnology, Ministry of Science and Technology, India, Department of Atomic Energy, Government of India, The Wellcome Trust DBT India Alliance, Science and Engineering Research Board
Life in Land
Openalex Percentile: Top 82%
Genomics and Phylogenetic Studies
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