SulA is able to block cell division in Escherichia coli by a mechanism different from sequestration

被引:7
作者
Vedyaykin, Alexey [1 ,2 ]
Rumyantseva, Natalia [1 ]
Khodorkovskii, Mikhail [1 ]
Vishnyakov, Innokentii [2 ]
机构
[1] Peter Great St Petersburg Polytech Univ, Polytech Skaya 29, St Petersburg 195251, Russia
[2] Russian Acad Sci, Inst Cytol, Tikhoretsky Ave 4, St Petersburg 194064, Russia
关键词
SOS response; Escherichia coli; Cell division; SulA; FtsZ; MOLECULE LOCALIZATION MICROSCOPY; FTSZ; SOS; PROTEIN; RING; POLYMERIZATION;
D O I
10.1016/j.bbrc.2020.03.012
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The SOS response is considered to be an extremely important feature of bacterial cells. It helps them to survive bad times, including helping to develop resistance to antibiotics. The SOS response blocks the cell division. For Escherichia coli it is well known that the SulA protein directly interacts with FtsZ - a key division protein. Now it is believed that fission blocking is based on FtsZ sequestration by the SulA protein, which leads to decrease in effective concentration of FtsZ in the cell below a critical value, which in vitro leads to dismantling of FtsZ polymers. In this work, we demonstrate that in order to block the division of E. coli, it is sufficient to have a relatively small amount of SulA in the cell. Moreover, the analysis of structures formed by FtsZ in E. coli cells under the conditions of SulA protein expression or the SOS response showed that there is no complete disassembly of FtsZ polymers, although Z-rings indeed are not formed. The results of the work indicate that the well-known sequestration mechanism is not comprehensive to explain blocking of the division process by SulA in vivo. (C) 2020 Elsevier Inc. All rights reserved.
引用
收藏
页码:948 / 953
页数:6
相关论文
共 26 条
  • [1] SOS, the formidable strategy of bacteria against aggressions
    Baharoglu, Zeynep
    Mazel, Didier
    [J]. FEMS MICROBIOLOGY REVIEWS, 2014, 38 (06) : 1126 - 1145
  • [2] Imaging intracellular fluorescent proteins at nanometer resolution
    Betzig, Eric
    Patterson, George H.
    Sougrat, Rachid
    Lindwasser, O. Wolf
    Olenych, Scott
    Bonifacino, Juan S.
    Davidson, Michael W.
    Lippincott-Schwartz, Jennifer
    Hess, Harald F.
    [J]. SCIENCE, 2006, 313 (5793) : 1642 - 1645
  • [3] In vivo organization of the FtsZ-ring by ZapA and ZapB revealed by quantitative super-resolution microscopy
    Buss, Jackson
    Coltharp, Carla
    Huang, Tao
    Pohlmeyer, Chris
    Wang, Shih-Chin
    Hatem, Christine
    Xiao, Jie
    [J]. MOLECULAR MICROBIOLOGY, 2013, 89 (06) : 1099 - 1120
  • [4] SulA Inhibits Assembly of FtsZ by a Simple Sequestration Mechanism
    Chen, Yaodong
    Milam, Sara L.
    Erickson, Harold P.
    [J]. BIOCHEMISTRY, 2012, 51 (14) : 3100 - 3109
  • [5] Investigation of regulation of FtsZ assembly by SulA and development of a model for FtsZ polymerization
    Dajkovic, Alex
    Mukherjee, Amit
    Lutkenhaus, Joe
    [J]. JOURNAL OF BACTERIOLOGY, 2008, 190 (07) : 2513 - 2526
  • [6] Ciprofloxacin Causes Persister Formation by Inducing the TisB toxin in Escherichia coli
    Doerr, Tobias
    Vulic, Marin
    Lewis, Kim
    [J]. PLOS BIOLOGY, 2010, 8 (02)
  • [7] At the Heart of Bacterial Cytokinesis: The Z Ring
    Du, Shishen
    Lutkenhaus, Joe
    [J]. TRENDS IN MICROBIOLOGY, 2019, 27 (09) : 781 - 791
  • [8] Art and artifacts in single-molecule localization microscopy: beyond attractive images
    Endesfelder, Ulrike
    Heilemann, Mike
    [J]. NATURE METHODS, 2014, 11 (03) : 235 - 238
  • [9] In Vivo Structure of the E. coli FtsZ-ring Revealed by Photoactivated Localization Microscopy (PALM)
    Guo Fu
    Tao Huang
    Buss, Jackson
    Coltharp, Carla
    Hensel, Zach
    Jie Xiao
    [J]. PLOS ONE, 2010, 5 (09): : 1 - 16
  • [10] High throughput 3D super-resolution microscopy reveals Caulobacter crescentus in vivo Z-ring organization
    Holden, Seamus J.
    Pengo, Thomas
    Meibom, Karin L.
    Fernandez, Carmen Fernandez
    Collier, Justine
    Manley, Suliana
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2014, 111 (12) : 4566 - 4571