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ORIGINAL RESEARCH article

Front. Microbiol.
Sec. Extreme Microbiology
Volume 15 - 2024 | doi: 10.3389/fmicb.2024.1441398
This article is part of the Research Topic Life Under Pressure: Microbial Adaptation and Survival in High Pressure Environments View all articles

N-terminus GTPase domain of the cytoskeleton protein FtsZ plays a critical role in its adaptation to high hydrostatic pressure

Provisionally accepted
Xue-Hua Cui Xue-Hua Cui 1,2Yu-Chen Wei Yu-Chen Wei 1Xue-Gong Li Xue-Gong Li 1,3Xiao-Qing Qi Xiao-Qing Qi 1,3L.F. Wu L.F. Wu 1,3,4Wei-Jia ZHANG Wei-Jia ZHANG 1,3*
  • 1 Laboratory of Deep-Sea microbial Cell Biology, Institute of Deep-Sea Science and Engineering, Chinese Academy of Sciences (CAS), Sanya, China
  • 2 University of Chinese Academy of Sciences, Beijing, Beijing, China
  • 3 Institution of Deep-sea Life Sciences, IDSSE-BGI, Hainan Deep-sea Technology Laboratory, Sanya, China
  • 4 UMR7283 Laboratoire de chimie bactérienne (LCB), Marseille, Provence-Alpes-Côte d'Azur, France

The final, formatted version of the article will be published soon.

    Studies in model microorganisms showed that cell division is highly vulnerable to high hydrostatic pressure (HHP). Disassembly of FtsZ filaments induced by HHP results in the failure of cell division and formation of filamentous cells in E. coli. The specific characteritics of FtsZ that allow for functional cell division in the deep-sea environments, especially in obligate piezophiles that grow exclusively under HHP condition, remain enigmatic. In this study, by using a self-developed HHP in-situ fixation apparatus, we compared the pressure tolerance of FtsZ proteins from pressure-sensitive strain Shewanella oneidensis MR-1 (FtsZSo) and obligately piezophilic strain Shewanella benthica DB21MT-2 (FtsZSb). We investigated the effect of HHP on FtsZ by examining the subcellular localization of GFP-tagged FtsZ in vivo and the filament of FtsZ in vitro. Our findings showed that, unlike FtsZSo, HHP hardly affected the Z-ring formation of FtsZSb, and filaments composed of FtsZSb were more stable after incubation under 50 MPa. By constructing chimeric and single amino acid mutated FtsZ proteins, we identified five residues in the N-terminal GTPase domain of FtsZSb whose mutation would impair the Z-ring formation under HHP conditions. Overall, these results demonstrate that FtsZ from the obligately piezophilic strain exhibits superior pressure tolerance than its homologues from shallow water species, both in vivo and in vitro. Differences in pressure tolerance of FtsZ are largely attributed to the N-terminal GTPase domain. This represents the first in-depth study of the adaptation of microbial cytoskeleton protein FtsZ to high hydrostatic pressure, which may provide insights into understanding the complex bioprocess of cell division under extreme environments.

    Keywords: ftsZ, Cell Division, Cytoskeleton, GTPase domain, high hydrostatic pressure, obligate piezophile into ftsZSo-N-gfp, ftsZSo-L-gfp and ftsZSo-C-gfp

    Received: 31 May 2024; Accepted: 30 Jul 2024.

    Copyright: © 2024 Cui, Wei, Li, Qi, Wu and ZHANG. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

    * Correspondence: Wei-Jia ZHANG, Laboratory of Deep-Sea microbial Cell Biology, Institute of Deep-Sea Science and Engineering, Chinese Academy of Sciences (CAS), Sanya, China

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