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

文献类型：期刊论文

作者Cui, Xue-Hua3,4; Wei, Yu-Chen4; Li, Xue-Gong2,4; Qi, Xiao-Qing2,4; Wu, Long-Fei1,2,4; Zhang, Wei-Jia2,4
刊名FRONTIERS IN MICROBIOLOGY
出版日期2024-08-16
卷号15页码:13
关键词obligate piezophile cell division cytoskeleton FtsZ high hydrostatic pressure GTPase domain
DOI10.3389/fmicb.2024.1441398
英文摘要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 characteristics 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 investigated the effect of HHP on FtsZ by examining the subcellular localization of GFP-tagged FtsZ in vivo and the stability of FtsZ filament in vitro. 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). 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 homologue 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.
WOS关键词POLYUNSATURATED FATTY-ACIDS ; Z-RING STRUCTURE ; ESCHERICHIA-COLI ; CELL-DIVISION ; IN-VIVO ; INDUCED DEPOLYMERIZATION ; PEPTIDOGLYCAN SYNTHESIS ; MORPHOLOGICAL CONTROL ; FUNCTIONAL ANALYSES ; DEEP
资助项目National Natural Science Foundation of China[NSFC4207612] ; National Natural Science Foundation of China[42176121] ; National Natural Science Foundation of China[91751108] ; Key Research and Development Program of Hainan Province[ZDKJ2021028] ; Strategic Priority Research Program of the Chinese Academy of Sciences[XDA19060403] ; Chinese Academy of Sciences
WOS研究方向Microbiology
语种英语
WOS记录号WOS:001302091900001
出版者FRONTIERS MEDIA SA
资助机构National Natural Science Foundation of China ; Key Research and Development Program of Hainan Province ; Strategic Priority Research Program of the Chinese Academy of Sciences ; Chinese Academy of Sciences
源URL[http://ir.idsse.ac.cn/handle/183446/11414]  
专题深海科学研究部_深海生物学研究室_深海微生物细胞生物学研究组
研究生部
通讯作者Zhang, Wei-Jia
作者单位1.Aix Marseille Univ, CNRS, LCB, Marseille, France
2.Inst Deep Sea Life Sci, IDSSE BGI, Sanya, Peoples R China
3.Univ Chinese Acad Sci, Coll Earth & Planetary Sci, Beijing, Peoples R China
4.Chinese Acad Sci, Lab Deep Sea Microbial Cell Biol, Inst Deep Sea Sci & Engn, Sanya, Peoples R China
推荐引用方式
GB/T 7714		 Cui, Xue-Hua,Wei, Yu-Chen,Li, Xue-Gong,et al. N-terminus GTPase domain of the cytoskeleton protein FtsZ plays a critical role in its adaptation to high hydrostatic pressure[J]. FRONTIERS IN MICROBIOLOGY,2024,15:13.
APA Cui, Xue-Hua,Wei, Yu-Chen,Li, Xue-Gong,Qi, Xiao-Qing,Wu, Long-Fei,&Zhang, Wei-Jia.(2024).N-terminus GTPase domain of the cytoskeleton protein FtsZ plays a critical role in its adaptation to high hydrostatic pressure.FRONTIERS IN MICROBIOLOGY,15,13.
MLA Cui, Xue-Hua,et al."N-terminus GTPase domain of the cytoskeleton protein FtsZ plays a critical role in its adaptation to high hydrostatic pressure".FRONTIERS IN MICROBIOLOGY 15(2024):13.

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来源：深海科学与工程研究所

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