ID | 65940 |
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Author |
Akıl, Caner
Research Institute for Interdisciplinary Science, Okayama University
Ali, Samson
Research Institute for Interdisciplinary Science, Okayama University
Tran, Linh T.
Research Institute for Interdisciplinary Science, Okayama University
Gaillard, Jérémie
University of Grenoble-Alpes, CEA, CNRS, INRA, Interdisciplinary Research Institute of Grenoble, Laboratoire de Physiologie Cellulaire & Végétale, CytoMorpho Lab
Li, Wenfei
National Laboratory of Solid State Microstructure, Department of Physics, Collaborative Innovation Center of Advanced Microstructures, Nanjing University
Hayashida, Kenichi
Cellular and Structural Physiology Institute (CeSPI), Nagoya University
Hirose, Mika
Institute for Protein Research, Osaka University
Kato, Takayuki
Institute for Protein Research, Osaka University
Oshima, Atsunori
Cellular and Structural Physiology Institute (CeSPI), Nagoya University
Fujishima, Kosuke
Tokyo Institute of Technology, Earth-Life Science Institute (ELSI)
Blanchoin, Laurent
University of Grenoble-Alpes, CEA, CNRS, INRA, Interdisciplinary Research Institute of Grenoble, Laboratoire de Physiologie Cellulaire & Végétale, CytoMorpho Lab
Narita, Akihiro
Division of Biological Science, Graduate School of Science, Nagoya University
Robinson, Robert C.
Research Institute for Interdisciplinary Science, Okayama University
ORCID
Kaken ID
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Abstract | Tubulins are critical for the internal organization of eukaryotic cells, and understanding their emergence is an important question in eukaryogenesis. Asgard archaea are the closest known prokaryotic relatives to eukaryotes. Here, we elucidated the apo and nucleotide-bound x-ray structures of an Asgard tubulin from hydrothermal living Odinarchaeota (OdinTubulin). The guanosine 5′-triphosphate (GTP)–bound structure resembles a microtubule protofilament, with GTP bound between subunits, coordinating the “+” end subunit through a network of water molecules and unexpectedly by two cations. A water molecule is located suitable for GTP hydrolysis. Time course crystallography and electron microscopy revealed conformational changes on GTP hydrolysis. OdinTubulin forms tubules at high temperatures, with short curved protofilaments coiling around the tubule circumference, more similar to FtsZ, rather than running parallel to its length, as in microtubules. Thus, OdinTubulin represents an evolutionary stage intermediate between prokaryotic FtsZ and eukaryotic microtubule-forming tubulins.
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Published Date | 2022-03-25
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Publication Title |
Science Advances
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Volume | volume8
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Issue | issue12
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Publisher | American Association for the Advancement of Science (AAAS)
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Start Page | eabm2225
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ISSN | 2375-2548
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Content Type |
Journal Article
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language |
English
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OAI-PMH Set |
岡山大学
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Copyright Holders | © 2022 The Authors
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File Version | publisher
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PubMed ID | |
DOI | |
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Related Url | isVersionOf https://doi.org/10.1126/sciadv.abm2225
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License | https://creativecommons.org/licenses/by-nc/4.0/
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Citation | Caner Akıl et al. ,Structure and dynamics of Odinarchaeota tubulin and the implications for eukaryotic microtubule evolution.Sci. Adv.8,eabm2225(2022).DOI:10.1126/sciadv.abm2225
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Funder Name |
Japan Science and Technology Agency
Japan Society for the Promotion of Science
Moore-Simons Project on the Origin of the Eukaryotic Cell
ELSI-First Logic Astrobiology Donation Program
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助成番号 | JPMJCR19S5
JP20H00476
GBMF9743
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