Please use this identifier to cite or link to this item: https://doi.org/10.1371/journal.pbio.1001389
Title: 3D-SIM Super Resolution Microscopy Reveals a Bead-Like Arrangement for FtsZ and the Division Machinery: Implications for Triggering Cytokinesis
Authors: Strauss M.P.
Liew A.T.F. 
Turnbull L.
Whitchurch C.B.
Monahan L.G.
Harry E.J.
Keywords: bacterial protein
EzrA protein
FtsZ protein
protein PBP2
unclassified drug
article
Bacillus subtilis
bacterial cell
cellular distribution
controlled study
cytokinesis
microscopy
nonhuman
protein function
protein localization
protein structure
Staphylococcus aureus
structure analysis
three dimensional structured illumination microscopy
Bacillus subtilis
Bacterial Proteins
Cytokinesis
Cytoskeletal Proteins
Green Fluorescent Proteins
Imaging, Three-Dimensional
Microbial Viability
Microscopy
Models, Biological
Movement
Protein Transport
Recombinant Fusion Proteins
Staphylococcus aureus
Time-Lapse Imaging
Bacillus subtilis
Bacteria (microorganisms)
Coccoidea
Posibacteria
Staphylococcus aureus
Issue Date: 2012
Citation: Strauss M.P., Liew A.T.F., Turnbull L., Whitchurch C.B., Monahan L.G., Harry E.J. (2012). 3D-SIM Super Resolution Microscopy Reveals a Bead-Like Arrangement for FtsZ and the Division Machinery: Implications for Triggering Cytokinesis. PLoS Biology 10 (9) : e1001389. ScholarBank@NUS Repository. https://doi.org/10.1371/journal.pbio.1001389
Abstract: FtsZ is a tubulin-like GTPase that is the major cytoskeletal protein in bacterial cell division. It polymerizes into a ring, called the Z ring, at the division site and acts as a scaffold to recruit other division proteins to this site as well as providing a contractile force for cytokinesis. To understand how FtsZ performs these functions, the in vivo architecture of the Z ring needs to be established, as well as how this structure constricts to enable cytokinesis. Conventional wide-field fluorescence microscopy depicts the Z ring as a continuous structure of uniform density. Here we use a form of super resolution microscopy, known as 3D-structured illumination microscopy (3D-SIM), to examine the architecture of the Z ring in cells of two Gram-positive organisms that have different cell shapes: the rod-shaped Bacillus subtilis and the coccoid Staphylococcus aureus. We show that in both organisms the Z ring is composed of a heterogeneous distribution of FtsZ. In addition, gaps of fluorescence were evident, which suggest that it is a discontinuous structure. Time-lapse studies using an advanced form of fast live 3D-SIM (Blaze) support a model of FtsZ localization within the Z ring that is dynamic and remains distributed in a heterogeneous manner. However, FtsZ dynamics alone do not trigger the constriction of the Z ring to allow cytokinesis. Lastly, we visualize other components of the divisome and show that they also adopt a bead-like localization pattern at the future division site. Our data lead us to propose that FtsZ guides the divisome to adopt a similar localization pattern to ensure Z ring constriction only proceeds following the assembly of a mature divisome. © 2012 Strauss et al.
Source Title: PLoS Biology
URI: https://scholarbank.nus.edu.sg/handle/10635/161634
ISSN: 15449173
DOI: 10.1371/journal.pbio.1001389
Appears in Collections:Elements
Staff Publications

Show full item record
Files in This Item:
File Description SizeFormatAccess SettingsVersion 
10_1371_journal_pbio_1001389.pdf1.63 MBAdobe PDF

OPEN

NoneView/Download

SCOPUSTM   
Citations

143
checked on Sep 21, 2020

Page view(s)

72
checked on Sep 18, 2020

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.