3D-SIM Super Resolution Microscopy Reveals a Bead-Like Arrangement for FtsZ and the Division Machinery: Implications for Triggering Cytokinesis

Strauss, MP; Liew, ATF; Turnbull, L; Whitchurch, CB; Monahan, LG; Harry, EJ

3D-SIM Super Resolution Microscopy Reveals a Bead-Like Arrangement for FtsZ and the Division Machinery: Implications for Triggering Cytokinesis

Strauss, MP Liew, ATF Turnbull, L

Whitchurch, CB

Monahan, LG

Harry, EJ

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Publication Type:: Journal Article
Citation:: PLoS Biology, 2012, 10 (9)
Issue Date:: 2012-09-01

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Field	Value	Language
dc.contributor.author	Strauss, MP	en_US
dc.contributor.author	Liew, ATF	en_US
dc.contributor.author	Turnbull, L https://orcid.org/0000-0002-9255-9033	en_US
dc.contributor.author	Whitchurch, CB https://orcid.org/0000-0003-2296-3791	en_US
dc.contributor.author	Monahan, LG https://orcid.org/0000-0003-2933-9000	en_US
dc.contributor.author	Harry, EJ https://orcid.org/0000-0003-0858-9473	en_US
dc.date.available	2012-08-03	en_US
dc.date.issued	2012-09-01	en_US
dc.identifier.citation	PLoS Biology, 2012, 10 (9)	en_US
dc.identifier.issn	1544-9173	en_US
dc.identifier.uri	http://hdl.handle.net/10453/53619
dc.description.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.	en_US
dc.relation	http://purl.org/au-research/grants/arc/DP0666670
dc.relation	http://purl.org/au-research/grants/nhmrc/GNT0571905
dc.relation.ispartof	PLoS Biology	en_US
dc.relation.isbasedon	10.1371/journal.pbio.1001389	en_US
dc.subject.classification	Developmental Biology	en_US
dc.subject.mesh	Bacillus subtilis	en_US
dc.subject.mesh	Staphylococcus aureus	en_US
dc.subject.mesh	Bacterial Proteins	en_US
dc.subject.mesh	Cytoskeletal Proteins	en_US
dc.subject.mesh	Green Fluorescent Proteins	en_US
dc.subject.mesh	Recombinant Fusion Proteins	en_US
dc.subject.mesh	Imaging, Three-Dimensional	en_US
dc.subject.mesh	Microscopy	en_US
dc.subject.mesh	Cytokinesis	en_US
dc.subject.mesh	Protein Transport	en_US
dc.subject.mesh	Movement	en_US
dc.subject.mesh	Models, Biological	en_US
dc.subject.mesh	Microbial Viability	en_US
dc.subject.mesh	Time-Lapse Imaging	en_US
dc.title	3D-SIM Super Resolution Microscopy Reveals a Bead-Like Arrangement for FtsZ and the Division Machinery: Implications for Triggering Cytokinesis	en_US
dc.type	Journal Article
utslib.citation.volume	9	en_US
utslib.citation.volume	10	en_US
utslib.for	0605 Microbiology	en_US
utslib.for	06 Biological Sciences	en_US
utslib.for	07 Agricultural and Veterinary Sciences	en_US
utslib.for	11 Medical and Health Sciences	en_US
pubs.embargo.period	Not known	en_US
pubs.organisational-group	/University of Technology Sydney
pubs.organisational-group	/University of Technology Sydney/Faculty of Science
pubs.organisational-group	/University of Technology Sydney/Strength - ithree - Institute of Infection, Immunity and Innovation
utslib.copyright.status	open_access
pubs.issue	9	en_US
pubs.publication-status	Published	en_US
pubs.volume	10	en_US

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.

Please use this identifier to cite or link to this item:

http://hdl.handle.net/10453/22178