• 文献检索
  • 文档翻译
  • 深度研究
  • 学术资讯
  • Suppr Zotero 插件Zotero 插件
  • 邀请有礼
  • 套餐&价格
  • 历史记录
应用&插件
Suppr Zotero 插件Zotero 插件浏览器插件Mac 客户端Windows 客户端微信小程序
定价
高级版会员购买积分包购买API积分包
服务
文献检索文档翻译深度研究API 文档MCP 服务
关于我们
关于 Suppr公司介绍联系我们用户协议隐私条款
关注我们

Suppr 超能文献

核心技术专利：CN118964589B侵权必究
粤ICP备2023148730 号-1Suppr @ 2026

文献检索

告别复杂PubMed语法，用中文像聊天一样搜索，搜遍4000万医学文献。AI智能推荐，让科研检索更轻松。

立即免费搜索

文件翻译

保留排版，准确专业，支持PDF/Word/PPT等文件格式，支持 12+语言互译。

免费翻译文档

深度研究

AI帮你快速写综述，25分钟生成高质量综述，智能提取关键信息，辅助科研写作。

立即免费体验

一种保守的细胞分裂蛋白直接调节丝状和单细胞放线菌中的 FtsZ 动力学。

A conserved cell division protein directly regulates FtsZ dynamics in filamentous and unicellular actinobacteria.

机构信息

Department of Molecular Microbiology, John Innes Centre, Norwich, United Kingdom.

Department of Cell and Developmental Biology, John Innes Centre, Norwich, United Kingdom.

出版信息

Elife. 2021 Mar 17;10:e63387. doi: 10.7554/eLife.63387.

DOI:10.7554/eLife.63387
PMID:33729912
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC7968930/
Abstract

Bacterial cell division is driven by the polymerization of the GTPase FtsZ into a contractile structure, the so-called Z-ring. This essential process involves proteins that modulate FtsZ dynamics and hence the overall Z-ring architecture. Actinobacteria like and lack known key FtsZ-regulators. Here we report the identification of SepH, a conserved actinobacterial protein that directly regulates FtsZ dynamics. We show that SepH is crucially involved in cell division in and that it binds FtsZ via a conserved helix-turn-helix motif, stimulating the assembly of FtsZ protofilaments. Comparative studies using the SepH homolog from further reveal that SepH can also bundle FtsZ protofilaments, indicating an additional Z-ring stabilizing function . We propose that SepH plays a crucial role at the onset of cytokinesis in actinobacteria by promoting the assembly of FtsZ filaments into division-competent Z-rings that can go on to mediate septum synthesis.

摘要

细菌细胞分裂是由 GTP 酶 FtsZ 聚合形成收缩结构（即所谓的 Z 环）驱动的。这个基本过程涉及调节 FtsZ 动力学的蛋白质，从而影响整个 Z 环结构。放线菌缺乏已知的关键 FtsZ 调节剂。在这里，我们报告了 SepH 的鉴定，这是一种保守的放线菌蛋白，可直接调节 FtsZ 的动力学。我们表明 SepH 对 和细胞分裂至关重要，它通过保守的螺旋-转角-螺旋基序与 FtsZ 结合，刺激 FtsZ 原丝的组装。使用来自 的 SepH 同源物进行的比较 研究进一步表明，SepH 还可以束状 FtsZ 原丝，表明其具有额外的 Z 环稳定功能。我们提出，SepH 通过促进 FtsZ 丝组装成有能力进行分裂的 Z 环，从而在放线菌细胞分裂开始时发挥关键作用，这些 Z 环可以继续介导隔膜合成。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/0a516ea09cdc/elife-63387-resp-fig2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/2fd4a9d5274f/elife-63387-fig1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/3636cdf284b7/elife-63387-fig1-figsupp1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/18e657d9ba4e/elife-63387-fig1-figsupp2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/5b7e904e1747/elife-63387-fig1-figsupp3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/aeacdcbacfa1/elife-63387-fig2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/dcbec5a6cc6a/elife-63387-fig2-figsupp1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/eb0fb09a0090/elife-63387-fig2-figsupp2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/23e4686ec0dd/elife-63387-fig3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/81a05d9a4bcc/elife-63387-fig3-figsupp1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/d3a2c3a0ad8d/elife-63387-fig3-figsupp2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/0e06d3e7a6b2/elife-63387-fig3-figsupp3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/a75a00ebf626/elife-63387-fig4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/9a79e447465e/elife-63387-fig4-figsupp1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/407ddd8f7150/elife-63387-fig5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/46b8e6595185/elife-63387-fig5-figsupp1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/cf61352d4f60/elife-63387-fig5-figsupp2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/9a633e22df43/elife-63387-fig5-figsupp3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/8ca4a8c017fb/elife-63387-fig5-figsupp4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/f07a69167fb2/elife-63387-fig5-figsupp5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/a054de4dc3c3/elife-63387-fig6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/10c8178b5f6a/elife-63387-fig6-figsupp1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/d506528ff886/elife-63387-fig6-figsupp2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/c6ba59d9e7f9/elife-63387-fig6-figsupp3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/997ac6ad04a7/elife-63387-fig7.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/30ce096db0ec/elife-63387-fig7-figsupp1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/5273160d2050/elife-63387-fig7-figsupp2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/df18d30f59de/elife-63387-fig7-figsupp3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/d72fccbf7b0a/elife-63387-fig7-figsupp4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/27f23892d595/elife-63387-fig7-figsupp5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/f844f6e81dc2/elife-63387-fig8.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/06a90260a8da/elife-63387-resp-fig1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/0a516ea09cdc/elife-63387-resp-fig2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/2fd4a9d5274f/elife-63387-fig1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/3636cdf284b7/elife-63387-fig1-figsupp1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/18e657d9ba4e/elife-63387-fig1-figsupp2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/5b7e904e1747/elife-63387-fig1-figsupp3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/aeacdcbacfa1/elife-63387-fig2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/dcbec5a6cc6a/elife-63387-fig2-figsupp1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/eb0fb09a0090/elife-63387-fig2-figsupp2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/23e4686ec0dd/elife-63387-fig3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/81a05d9a4bcc/elife-63387-fig3-figsupp1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/d3a2c3a0ad8d/elife-63387-fig3-figsupp2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/0e06d3e7a6b2/elife-63387-fig3-figsupp3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/a75a00ebf626/elife-63387-fig4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/9a79e447465e/elife-63387-fig4-figsupp1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/407ddd8f7150/elife-63387-fig5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/46b8e6595185/elife-63387-fig5-figsupp1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/cf61352d4f60/elife-63387-fig5-figsupp2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/9a633e22df43/elife-63387-fig5-figsupp3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/8ca4a8c017fb/elife-63387-fig5-figsupp4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/f07a69167fb2/elife-63387-fig5-figsupp5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/a054de4dc3c3/elife-63387-fig6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/10c8178b5f6a/elife-63387-fig6-figsupp1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/d506528ff886/elife-63387-fig6-figsupp2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/c6ba59d9e7f9/elife-63387-fig6-figsupp3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/997ac6ad04a7/elife-63387-fig7.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/30ce096db0ec/elife-63387-fig7-figsupp1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/5273160d2050/elife-63387-fig7-figsupp2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/df18d30f59de/elife-63387-fig7-figsupp3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/d72fccbf7b0a/elife-63387-fig7-figsupp4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/27f23892d595/elife-63387-fig7-figsupp5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/f844f6e81dc2/elife-63387-fig8.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/06a90260a8da/elife-63387-resp-fig1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4060/7968930/0a516ea09cdc/elife-63387-resp-fig2.jpg

相似文献

1
A conserved cell division protein directly regulates FtsZ dynamics in filamentous and unicellular actinobacteria.一种保守的细胞分裂蛋白直接调节丝状和单细胞放线菌中的 FtsZ 动力学。
Elife. 2021 Mar 17;10:e63387. doi: 10.7554/eLife.63387.
2
Specific amino acid substitutions in β strand S2 of FtsZ cause spiraling septation and impair assembly cooperativity in Streptomyces spp.β 链 S2 中的特定氨基酸取代会导致螺旋状的分隔，并损害链霉菌属中装配的协同性。
Mol Microbiol. 2019 Jul;112(1):184-198. doi: 10.1111/mmi.14262. Epub 2019 May 17.
3
Mutation of G51 in SepF impairs FtsZ assembly promoting ability of SepF and retards the division of cells.G51 突变使 SepF 丧失促进 FtsZ 组装的能力，并延缓细胞分裂。
Biochem J. 2018 Aug 14;475(15):2473-2489. doi: 10.1042/BCJ20180281.
4
FtsA Regulates Z-Ring Morphology and Cell Wall Metabolism in an FtsZ C-Terminal Linker-Dependent Manner in Caulobacter crescentus.FtsA 通过依赖于 FtsZ C 端连接子的方式调节 Z 环形态和细胞壁代谢在新月柄杆菌中。
J Bacteriol. 2020 Mar 11;202(7). doi: 10.1128/JB.00693-19.
5
Genetic evidence that mycobacterial FtsZ and FtsW proteins interact, and colocalize to the division site in Mycobacterium smegmatis.分枝杆菌FtsZ和FtsW蛋白相互作用并共定位于耻垢分枝杆菌分裂位点的遗传学证据。
FEMS Microbiol Lett. 2005 Sep 1;250(1):9-17. doi: 10.1016/j.femsle.2005.06.043.
6
Glutamate 83 and arginine 85 of helix H3 bend are key residues for FtsZ polymerization, GTPase activity and cellular viability of Escherichia coli: lateral mutations affect FtsZ polymerization and E. coli viability.螺旋 H3 上的谷氨酸 83 和精氨酸 85 是 FtsZ 聚合、GTP 酶活性和大肠杆菌细胞活力的关键残基：侧链突变会影响 FtsZ 聚合和大肠杆菌的活力。
BMC Microbiol. 2013 Feb 5;13:26. doi: 10.1186/1471-2180-13-26.
7
Two dynamin-like proteins stabilize FtsZ rings during sporulation.两种动力蛋白样蛋白在孢子形成过程中稳定 FtsZ 环。
Proc Natl Acad Sci U S A. 2017 Jul 25;114(30):E6176-E6183. doi: 10.1073/pnas.1704612114. Epub 2017 Jul 7.
8
Influence of core divisome proteins on cell division in ATCC 10712.核心 divisome 蛋白对 ATCC 10712 细胞分裂的影响。
Microbiology (Reading). 2021 Feb;167(2). doi: 10.1099/mic.0.001015.
9
WhmD promotes the assembly of Mycobacterium smegmatis FtsZ: A possible role of WhmD in bacterial cell division.WhmD促进耻垢分枝杆菌FtsZ的组装：WhmD在细菌细胞分裂中的可能作用。
Int J Biol Macromol. 2017 Feb;95:582-591. doi: 10.1016/j.ijbiomac.2016.11.056. Epub 2016 Nov 19.
10
Essential dynamic interdependence of FtsZ and SepF for Z-ring and septum formation in Corynebacterium glutamicum.在谷氨酸棒杆菌中，FtsZ 和 SepF 对于 Z 环和隔膜形成的基本动态相互依赖。
Nat Commun. 2020 Apr 2;11(1):1641. doi: 10.1038/s41467-020-15490-8.

引用本文的文献

1
Peptidoglycan-reshuffling proteins SCO0954, SCO1758, SCO4439, and SCO4440 modulate the formation of wall-deficient cells in Streptomyces coelicolor under hyperosmotic sucrose stress.肽聚糖重排蛋白SCO0954、SCO1758、SCO4439和SCO4440在高渗蔗糖胁迫下调节天蓝色链霉菌中细胞壁缺陷型细胞的形成。
Sci Rep. 2025 Sep 1;15(1):32112. doi: 10.1038/s41598-025-15457-z.
2
Function and firing of the contractile injection system requires the membrane protein CisA.收缩性注射系统的功能和激发需要膜蛋白CisA。
Elife. 2025 Jul 8;14:RP104064. doi: 10.7554/eLife.104064.
3
Morphology-engineered alleviation of mycelial aggregation in chassis for potentiated production of secondary metabolites.

本文引用的文献

1
FtsZ treadmilling is essential for Z-ring condensation and septal constriction initiation in Bacillus subtilis cell division.在枯草芽孢杆菌的细胞分裂中，FtsZ treadmilling 对于 Z 环的浓缩和隔膜收缩的起始是必不可少的。
Nat Commun. 2021 Apr 27;12(1):2448. doi: 10.1038/s41467-021-22526-0.
2
Single-molecule imaging reveals that Z-ring condensation is essential for cell division in Bacillus subtilis.单分子成像揭示了 Z 环凝聚对于枯草芽孢杆菌细胞分裂的重要性。
Nat Microbiol. 2021 May;6(5):553-562. doi: 10.1038/s41564-021-00878-z. Epub 2021 Mar 18.
3
Progression of the late-stage divisome is unaffected by the depletion of the cytoplasmic FtsZ pool.
形态工程化减轻底盘中菌丝体聚集以增强次级代谢产物的生产。
Synth Syst Biotechnol. 2025 May 26;10(3):1059-1069. doi: 10.1016/j.synbio.2025.05.010. eCollection 2025 Sep.
4
How do spherical bacteria regulate cell division?球形细菌如何调节细胞分裂？
Biochem Soc Trans. 2025 Apr 17;53(2):447-60. doi: 10.1042/BST20240956.
5
Microbe Profile: a model species to study morphology and differentiation in filamentous bacteria.微生物简介：一种用于研究丝状细菌形态和分化的模式物种。
Microbiology (Reading). 2025 Mar;171(3). doi: 10.1099/mic.0.001541.
6
A dispensable SepIVA orthologue in Streptomyces venezuelae is associated with polar growth and not cell division.委内瑞拉链霉菌中一个可有可无的 SepIVA 同源物与极性生长而非细胞分裂有关。
BMC Microbiol. 2024 Nov 18;24(1):481. doi: 10.1186/s12866-024-03625-6.
7
Tip extension and simultaneous multiple fission in a filamentous bacterium.丝状细菌的顶体延伸和同时的多重裂变。
Proc Natl Acad Sci U S A. 2024 Sep 10;121(37):e2408654121. doi: 10.1073/pnas.2408654121. Epub 2024 Sep 3.
8
Eukaryotic-like gephyrin and cognate membrane receptor coordinate corynebacterial cell division and polar elongation.真核样小胶蛋白和同源膜受体协调棒状杆菌的细胞分裂和极性伸长。
Nat Microbiol. 2023 Oct;8(10):1896-1910. doi: 10.1038/s41564-023-01473-0. Epub 2023 Sep 7.
9
The Best of Both Worlds-Streptomyces coelicolor and Streptomyces venezuelae as Model Species for Studying Antibiotic Production and Bacterial Multicellular Development.两全其美——链霉菌属和委内瑞拉链霉菌作为研究抗生素产生和细菌多细胞发育的模式种。
J Bacteriol. 2023 Jul 25;205(7):e0015323. doi: 10.1128/jb.00153-23. Epub 2023 Jun 22.
10
MipZ caps the plus-end of FtsZ polymers to promote their rapid disassembly.MipZ 在 FtsZ 聚合物的正端加上帽子以促进其快速解体。
Proc Natl Acad Sci U S A. 2022 Dec 13;119(50):e2208227119. doi: 10.1073/pnas.2208227119. Epub 2022 Dec 9.
后期分裂体的进展不受细胞质 FtsZ 池耗尽的影响。
Commun Biol. 2021 Mar 1;4(1):270. doi: 10.1038/s42003-021-01789-9.
4
Influence of core divisome proteins on cell division in ATCC 10712.核心 divisome 蛋白对 ATCC 10712 细胞分裂的影响。
Microbiology (Reading). 2021 Feb;167(2). doi: 10.1099/mic.0.001015.
5
The speed of FtsZ treadmilling is tightly regulated by membrane binding.FtsZ 环的 treadmilling 速度受到膜结合的严格调控。
Sci Rep. 2020 Jun 26;10(1):10447. doi: 10.1038/s41598-020-67224-x.
6
Insights into the Structure, Function, and Dynamics of the Bacterial Cytokinetic FtsZ-Ring.细菌细胞分裂 FtsZ 环的结构、功能和动力学的深入了解。
Annu Rev Biophys. 2020 May 6;49:309-341. doi: 10.1146/annurev-biophys-121219-081703. Epub 2020 Feb 24.
7
Cooperative ordering of treadmilling filaments in cytoskeletal networks of FtsZ and its crosslinker ZapA.FtsZ 和其交联蛋白 ZapA 组成的细胞骨架网络中踏车丝状肌动蛋白的协同组装。
Nat Commun. 2019 Dec 17;10(1):5744. doi: 10.1038/s41467-019-13702-4.
8
RocS drives chromosome segregation and nucleoid protection in Streptococcus pneumoniae.RocS 驱动肺炎链球菌的染色体分离和核区保护。
Nat Microbiol. 2019 Oct;4(10):1661-1670. doi: 10.1038/s41564-019-0472-z. Epub 2019 Jun 10.
9
Specific amino acid substitutions in β strand S2 of FtsZ cause spiraling septation and impair assembly cooperativity in Streptomyces spp.β 链 S2 中的特定氨基酸取代会导致螺旋状的分隔，并损害链霉菌属中装配的协同性。
Mol Microbiol. 2019 Jul;112(1):184-198. doi: 10.1111/mmi.14262. Epub 2019 May 17.
10
Interactive Tree Of Life (iTOL) v4: recent updates and new developments.交互式生命树 (iTOL) v4：最新更新和新发展。
Nucleic Acids Res. 2019 Jul 2;47(W1):W256-W259. doi: 10.1093/nar/gkz239.