---
_id: '14280'
abstract:
- lang: eng
text: "Cell division in Escherichia coli is performed by the divisome, a multi-protein
complex composed of more than 30 proteins. The divisome spans from the cytoplasm
through the inner membrane to the cell wall and the outer membrane. Divisome assembly
is initiated by a cytoskeletal structure, the so-called Z-ring, which localizes
at the center of the E. coli cell and determines the position of the future cell
septum. The Z-ring is composed of the highly conserved bacterial tubulin homologue
FtsZ, which forms treadmilling filaments. These filaments are recruited to the
inner membrane by FtsA, a highly conserved bacterial actin homologue. FtsA interacts
with other proteins in the periplasm and thus connects the cytoplasmic and periplasmic
components of the divisome. \r\nA previous model postulated that FtsA regulates
maturation of the divisome by switching from an oligomeric, inactive state to
a monomeric and active state. This model was based mostly on in vivo studies,
as a biochemical characterization of FtsA has been hampered by difficulties in
purifying the protein. Here, we studied FtsA using an in vitro reconstitution
approach and aimed to answer two questions: (i) How are dynamics from cytoplasmic,
treadmilling FtsZ filaments coupled to proteins acting in the periplasmic space
and (ii) How does FtsA regulate the maturation of the divisome?\r\nWe found that
the cytoplasmic peptides of the transmembrane proteins FtsN and FtsQ interact
directly with FtsA and can follow the spatiotemporal signal of FtsA/Z filaments.
When we investigated the underlying mechanism by imaging single molecules of FtsNcyto,
we found the peptide to interact transiently with FtsA. An in depth analysis of
the single molecule trajectories helped to postulate a model where PG synthases
follow the dynamics of FtsZ by a diffusion and capture mechanism. \r\nFollowing
up on these findings we were interested in how the self-interaction of FtsA changes
when it encounters FtsNcyto and if we can confirm the proposed oligomer-monomer
switch. For this, we compared the behavior of the previously identified, hyperactive
mutant FtsA R286W with wildtype FtsA. The mutant outperforms WT in mirroring and
transmitting the spatiotemporal signal of treadmilling FtsZ filaments. Surprisingly
however, we found that this was not due to a difference in the self-interaction
strength of the two variants, but a difference in their membrane residence time.
Furthermore, in contrast to our expectations, upon binding of FtsNcyto the measured
self-interaction of FtsA actually increased. \r\nWe propose that FtsNcyto induces
a rearrangement of the oligomeric architecture of FtsA. In further consequence
this change leads to more persistent FtsZ filaments which results in a defined
signalling zone, allowing formation of the mature divisome. The observed difference
between FtsA WT and R286W is due to the vastly different membrane turnover of
the proteins. R286W cycles 5-10x faster compared to WT which allows to sample
FtsZ filaments at faster frequencies. These findings can explain the observed
differences in toxicity for overexpression of FtsA WT and R286W and help to understand
how FtsA regulates divisome maturation."
acknowledged_ssus:
- _id: Bio
- _id: LifeSc
alternative_title:
- ISTA Thesis
article_processing_charge: No
author:
- first_name: Philipp
full_name: Radler, Philipp
id: 40136C2A-F248-11E8-B48F-1D18A9856A87
last_name: Radler
orcid: '0000-0001-9198-2182 '
citation:
ama: Radler P. Spatiotemporal signaling during assembly of the bacterial divisome.
2023. doi:10.15479/at:ista:14280
apa: Radler, P. (2023). Spatiotemporal signaling during assembly of the bacterial
divisome. Institute of Science and Technology Austria. https://doi.org/10.15479/at:ista:14280
chicago: Radler, Philipp. “Spatiotemporal Signaling during Assembly of the Bacterial
Divisome.” Institute of Science and Technology Austria, 2023. https://doi.org/10.15479/at:ista:14280.
ieee: P. Radler, “Spatiotemporal signaling during assembly of the bacterial divisome,”
Institute of Science and Technology Austria, 2023.
ista: Radler P. 2023. Spatiotemporal signaling during assembly of the bacterial
divisome. Institute of Science and Technology Austria.
mla: Radler, Philipp. Spatiotemporal Signaling during Assembly of the Bacterial
Divisome. Institute of Science and Technology Austria, 2023, doi:10.15479/at:ista:14280.
short: P. Radler, Spatiotemporal Signaling during Assembly of the Bacterial Divisome,
Institute of Science and Technology Austria, 2023.
date_created: 2023-09-06T10:58:25Z
date_published: 2023-09-25T00:00:00Z
date_updated: 2024-02-21T12:35:18Z
day: '25'
ddc:
- '572'
degree_awarded: PhD
department:
- _id: GradSch
- _id: MaLo
doi: 10.15479/at:ista:14280
ec_funded: 1
file:
- access_level: closed
checksum: 87eef11fbc5c7df0826f12a3a629b444
content_type: application/vnd.openxmlformats-officedocument.wordprocessingml.document
creator: pradler
date_created: 2023-10-04T10:11:53Z
date_updated: 2023-10-04T10:28:35Z
file_id: '14390'
file_name: PhD Thesis_Philipp Radler_20231004.docx
file_size: 114932847
relation: source_file
- access_level: closed
checksum: 3253e099b7126469d941fd9419d68b4f
content_type: application/pdf
creator: pradler
date_created: 2023-10-04T10:11:21Z
date_updated: 2023-10-04T10:28:35Z
embargo: 2024-10-04
embargo_to: open_access
file_id: '14391'
file_name: PhD Thesis_Philipp Radler_20231004.pdf
file_size: 37838778
relation: main_file
file_date_updated: 2023-10-04T10:28:35Z
has_accepted_license: '1'
keyword:
- Cell Division
- Reconstitution
- FtsZ
- FtsA
- Divisome
- E.coli
language:
- iso: eng
month: '09'
oa_version: Published Version
page: '156'
project:
- _id: 2595697A-B435-11E9-9278-68D0E5697425
call_identifier: H2020
grant_number: '679239'
name: Self-Organization of the Bacterial Cell
- _id: fc38323b-9c52-11eb-aca3-ff8afb4a011d
grant_number: P34607
name: "Understanding bacterial cell division by in vitro\r\nreconstitution"
- _id: 2596EAB6-B435-11E9-9278-68D0E5697425
grant_number: ALTF 2015-1163
name: Synthesis of bacterial cell wall
- _id: 259B655A-B435-11E9-9278-68D0E5697425
grant_number: LT000824/2016
name: Reconstitution of bacterial cell wall sythesis
publication_identifier:
isbn:
- 978-3-99078-033-6
issn:
- 2663-337X
publication_status: published
publisher: Institute of Science and Technology Austria
related_material:
record:
- id: '11373'
relation: part_of_dissertation
status: public
- id: '7387'
relation: part_of_dissertation
status: public
- id: '10934'
relation: research_data
status: public
status: public
supervisor:
- first_name: Martin
full_name: Loose, Martin
id: 462D4284-F248-11E8-B48F-1D18A9856A87
last_name: Loose
orcid: 0000-0001-7309-9724
title: Spatiotemporal signaling during assembly of the bacterial divisome
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: dissertation
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
year: '2023'
...
---
_id: '9243'
abstract:
- lang: eng
text: Peptidoglycan is an essential component of the bacterial cell envelope that
surrounds the cytoplasmic membrane to protect the cell from osmotic lysis. Important
antibiotics such as β-lactams and glycopeptides target peptidoglycan biosynthesis.
Class A penicillin-binding proteins (PBPs) are bifunctional membrane-bound peptidoglycan
synthases that polymerize glycan chains and connect adjacent stem peptides by
transpeptidation. How these enzymes work in their physiological membrane environment
is poorly understood. Here, we developed a novel Förster resonance energy transfer-based
assay to follow in real time both reactions of class A PBPs reconstituted in liposomes
or supported lipid bilayers and applied this assay with PBP1B homologues from
Escherichia coli, Pseudomonas aeruginosa, and Acinetobacter baumannii in the presence
or absence of their cognate lipoprotein activator. Our assay will allow unravelling
the mechanisms of peptidoglycan synthesis in a lipid-bilayer environment and can
be further developed to be used for high-throughput screening for new antimicrobials.
acknowledgement: 'We thank Alexander Egan (Newcastle University) for purified proteins
LpoB(sol) and LpoPPa(sol), Federico Corona (Newcastle University) for purified MepM,
and Oliver Birkholz and Jacob Piehler (Department of Biology and Center of Cellular
Nanoanalytics, University of Osnabru¨ ck) for their help with PBP1B reconstitution
into polymer-SLBs and initial guidance on single particle tracking. We also acknowledge
Christian P Richter and Changjiang You (Department of Biology and Center of Cellular
Nanoanalytics, University of Osnabru¨ ck) for providing SLIMfast software and tris-DODA-NTA
reagent, respectively. This work was funded by the BBSRC grant BB/R017409/1 (to
WV), the European Research Council through grant ERC-2015-StG-679239 (to ML), and
long-term fellowships HFSP LT 000824/2016-L4 and EMBO ALTF 1163–2015 (to NB). '
article_number: 1-32
article_processing_charge: No
article_type: original
author:
- first_name: Víctor M.
full_name: Hernández-Rocamora, Víctor M.
last_name: Hernández-Rocamora
- first_name: Natalia S.
full_name: Baranova, Natalia S.
id: 38661662-F248-11E8-B48F-1D18A9856A87
last_name: Baranova
orcid: 0000-0002-3086-9124
- first_name: Katharina
full_name: Peters, Katharina
last_name: Peters
- first_name: Eefjan
full_name: Breukink, Eefjan
last_name: Breukink
- first_name: Martin
full_name: Loose, Martin
id: 462D4284-F248-11E8-B48F-1D18A9856A87
last_name: Loose
orcid: 0000-0001-7309-9724
- first_name: Waldemar
full_name: Vollmer, Waldemar
last_name: Vollmer
citation:
ama: Hernández-Rocamora VM, Baranova NS, Peters K, Breukink E, Loose M, Vollmer
W. Real time monitoring of peptidoglycan synthesis by membrane-reconstituted penicillin
binding proteins. eLife. 2021;10. doi:10.7554/eLife.61525
apa: Hernández-Rocamora, V. M., Baranova, N. S., Peters, K., Breukink, E., Loose,
M., & Vollmer, W. (2021). Real time monitoring of peptidoglycan synthesis
by membrane-reconstituted penicillin binding proteins. ELife. eLife Sciences
Publications. https://doi.org/10.7554/eLife.61525
chicago: Hernández-Rocamora, Víctor M., Natalia S. Baranova, Katharina Peters, Eefjan
Breukink, Martin Loose, and Waldemar Vollmer. “Real Time Monitoring of Peptidoglycan
Synthesis by Membrane-Reconstituted Penicillin Binding Proteins.” ELife.
eLife Sciences Publications, 2021. https://doi.org/10.7554/eLife.61525.
ieee: V. M. Hernández-Rocamora, N. S. Baranova, K. Peters, E. Breukink, M. Loose,
and W. Vollmer, “Real time monitoring of peptidoglycan synthesis by membrane-reconstituted
penicillin binding proteins,” eLife, vol. 10. eLife Sciences Publications,
2021.
ista: Hernández-Rocamora VM, Baranova NS, Peters K, Breukink E, Loose M, Vollmer
W. 2021. Real time monitoring of peptidoglycan synthesis by membrane-reconstituted
penicillin binding proteins. eLife. 10, 1–32.
mla: Hernández-Rocamora, Víctor M., et al. “Real Time Monitoring of Peptidoglycan
Synthesis by Membrane-Reconstituted Penicillin Binding Proteins.” ELife,
vol. 10, 1–32, eLife Sciences Publications, 2021, doi:10.7554/eLife.61525.
short: V.M. Hernández-Rocamora, N.S. Baranova, K. Peters, E. Breukink, M. Loose,
W. Vollmer, ELife 10 (2021).
date_created: 2021-03-14T23:01:33Z
date_published: 2021-02-24T00:00:00Z
date_updated: 2023-08-07T14:10:50Z
day: '24'
ddc:
- '570'
department:
- _id: MaLo
doi: 10.7554/eLife.61525
ec_funded: 1
external_id:
isi:
- '000627596400001'
file:
- access_level: open_access
checksum: 79897a09bfecd9914d39c4aea2841855
content_type: application/pdf
creator: dernst
date_created: 2021-03-22T07:36:08Z
date_updated: 2021-03-22T07:36:08Z
file_id: '9268'
file_name: 2021_eLife_HernandezRocamora.pdf
file_size: 2314698
relation: main_file
success: 1
file_date_updated: 2021-03-22T07:36:08Z
has_accepted_license: '1'
intvolume: ' 10'
isi: 1
language:
- iso: eng
month: '02'
oa: 1
oa_version: Published Version
project:
- _id: 2595697A-B435-11E9-9278-68D0E5697425
call_identifier: H2020
grant_number: '679239'
name: Self-Organization of the Bacterial Cell
- _id: 2596EAB6-B435-11E9-9278-68D0E5697425
grant_number: ALTF 2015-1163
name: Synthesis of bacterial cell wall
- _id: 259B655A-B435-11E9-9278-68D0E5697425
grant_number: LT000824/2016
name: Reconstitution of bacterial cell wall sythesis
publication: eLife
publication_identifier:
eissn:
- 2050-084X
publication_status: published
publisher: eLife Sciences Publications
quality_controlled: '1'
scopus_import: '1'
status: public
title: Real time monitoring of peptidoglycan synthesis by membrane-reconstituted penicillin
binding proteins
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 10
year: '2021'
...
---
_id: '7387'
abstract:
- lang: eng
text: Most bacteria accomplish cell division with the help of a dynamic protein
complex called the divisome, which spans the cell envelope in the plane of division.
Assembly and activation of this machinery are coordinated by the tubulin-related
GTPase FtsZ, which was found to form treadmilling filaments on supported bilayers
in vitro1, as well as in live cells, in which filaments circle around the cell
division site2,3. Treadmilling of FtsZ is thought to actively move proteins around
the division septum, thereby distributing peptidoglycan synthesis and coordinating
the inward growth of the septum to form the new poles of the daughter cells4.
However, the molecular mechanisms underlying this function are largely unknown.
Here, to study how FtsZ polymerization dynamics are coupled to downstream proteins,
we reconstituted part of the bacterial cell division machinery using its purified
components FtsZ, FtsA and truncated transmembrane proteins essential for cell
division. We found that the membrane-bound cytosolic peptides of FtsN and FtsQ
co-migrated with treadmilling FtsZ–FtsA filaments, but despite their directed
collective behaviour, individual peptides showed random motion and transient confinement.
Our work suggests that divisome proteins follow treadmilling FtsZ filaments by
a diffusion-and-capture mechanism, which can give rise to a moving zone of signalling
activity at the division site.
acknowledgement: We acknowledge members of the Loose laboratory at IST Austria for
helpful discussions—in particular, P. Caldas for help with the treadmilling analysis,
M. Jimenez, A. Raso and N. Ropero for providing Alexa Fluor 488- and Alexa Fluor
647-labelled FtsA for the MST and analytical ultracentrifugation experiments. We
thank C. You for providing the DODA-tris-NTA phospholipids, as well as J. Piehler
and C. Richter (Department of Biology, University of Osnabruck, Germany) for the
SLIMfast single-molecule tracking software and help with the confinement analysis.
We thank J. Errington and H. Murray (both at Newcastle University, UK) for critical
reading of the manuscript, and J. Brugués (MPI-CBG and MPI-PKS, Dresden, Germany)
for help with the MATLAB programming and reading of the manuscript. This work was
supported by the European Research Council through grant ERC-2015-StG-679239 to
M.L. and grants HFSP LT 000824/2016-L4 and EMBO ALTF 1163-2015 to N.B., a grant
from the Ministry of Economy and Competitiveness of the Spanish Government (BFU2016-75471-C2-1-P)
to C.A. and G.R., and a Wellcome Trust Senior Investigator award (101824/Z/13/Z)
and a grant from the BBSRC (BB/R017409/1) to W.V.
article_processing_charge: No
article_type: letter_note
author:
- first_name: Natalia S.
full_name: Baranova, Natalia S.
id: 38661662-F248-11E8-B48F-1D18A9856A87
last_name: Baranova
orcid: 0000-0002-3086-9124
- first_name: Philipp
full_name: Radler, Philipp
id: 40136C2A-F248-11E8-B48F-1D18A9856A87
last_name: Radler
orcid: '0000-0001-9198-2182 '
- first_name: Víctor M.
full_name: Hernández-Rocamora, Víctor M.
last_name: Hernández-Rocamora
- first_name: Carlos
full_name: Alfonso, Carlos
last_name: Alfonso
- first_name: Maria D
full_name: Lopez Pelegrin, Maria D
id: 319AA9CE-F248-11E8-B48F-1D18A9856A87
last_name: Lopez Pelegrin
- first_name: Germán
full_name: Rivas, Germán
last_name: Rivas
- first_name: Waldemar
full_name: Vollmer, Waldemar
last_name: Vollmer
- first_name: Martin
full_name: Loose, Martin
id: 462D4284-F248-11E8-B48F-1D18A9856A87
last_name: Loose
orcid: 0000-0001-7309-9724
citation:
ama: Baranova NS, Radler P, Hernández-Rocamora VM, et al. Diffusion and capture
permits dynamic coupling between treadmilling FtsZ filaments and cell division
proteins. Nature Microbiology. 2020;5:407-417. doi:10.1038/s41564-019-0657-5
apa: Baranova, N. S., Radler, P., Hernández-Rocamora, V. M., Alfonso, C., Lopez
Pelegrin, M. D., Rivas, G., … Loose, M. (2020). Diffusion and capture permits
dynamic coupling between treadmilling FtsZ filaments and cell division proteins.
Nature Microbiology. Springer Nature. https://doi.org/10.1038/s41564-019-0657-5
chicago: Baranova, Natalia S., Philipp Radler, Víctor M. Hernández-Rocamora, Carlos
Alfonso, Maria D Lopez Pelegrin, Germán Rivas, Waldemar Vollmer, and Martin Loose.
“Diffusion and Capture Permits Dynamic Coupling between Treadmilling FtsZ Filaments
and Cell Division Proteins.” Nature Microbiology. Springer Nature, 2020.
https://doi.org/10.1038/s41564-019-0657-5.
ieee: N. S. Baranova et al., “Diffusion and capture permits dynamic coupling
between treadmilling FtsZ filaments and cell division proteins,” Nature Microbiology,
vol. 5. Springer Nature, pp. 407–417, 2020.
ista: Baranova NS, Radler P, Hernández-Rocamora VM, Alfonso C, Lopez Pelegrin MD,
Rivas G, Vollmer W, Loose M. 2020. Diffusion and capture permits dynamic coupling
between treadmilling FtsZ filaments and cell division proteins. Nature Microbiology.
5, 407–417.
mla: Baranova, Natalia S., et al. “Diffusion and Capture Permits Dynamic Coupling
between Treadmilling FtsZ Filaments and Cell Division Proteins.” Nature Microbiology,
vol. 5, Springer Nature, 2020, pp. 407–17, doi:10.1038/s41564-019-0657-5.
short: N.S. Baranova, P. Radler, V.M. Hernández-Rocamora, C. Alfonso, M.D. Lopez
Pelegrin, G. Rivas, W. Vollmer, M. Loose, Nature Microbiology 5 (2020) 407–417.
date_created: 2020-01-28T16:14:41Z
date_published: 2020-01-20T00:00:00Z
date_updated: 2023-10-06T12:22:38Z
day: '20'
department:
- _id: MaLo
doi: 10.1038/s41564-019-0657-5
ec_funded: 1
external_id:
isi:
- '000508584700007'
pmid:
- '31959972'
intvolume: ' 5'
isi: 1
language:
- iso: eng
main_file_link:
- open_access: '1'
url: http://europepmc.org/article/PMC/7048620
month: '01'
oa: 1
oa_version: Submitted Version
page: 407-417
pmid: 1
project:
- _id: 2595697A-B435-11E9-9278-68D0E5697425
call_identifier: H2020
grant_number: '679239'
name: Self-Organization of the Bacterial Cell
- _id: 259B655A-B435-11E9-9278-68D0E5697425
grant_number: LT000824/2016
name: Reconstitution of bacterial cell wall sythesis
- _id: 2596EAB6-B435-11E9-9278-68D0E5697425
grant_number: ALTF 2015-1163
name: Synthesis of bacterial cell wall
publication: Nature Microbiology
publication_identifier:
issn:
- 2058-5276
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
related_material:
link:
- description: News on IST Homepage
relation: press_release
url: https://ist.ac.at/en/news/little-cell-big-cover-story/
record:
- id: '14280'
relation: dissertation_contains
status: public
scopus_import: '1'
status: public
title: Diffusion and capture permits dynamic coupling between treadmilling FtsZ filaments
and cell division proteins
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 5
year: '2020'
...
---
_id: '1213'
abstract:
- lang: eng
text: Bacterial cytokinesis is commonly initiated by the Z-ring, a dynamic cytoskeletal
structure that assembles at the site of division. Its primary component is FtsZ,
a tubulin-like GTPase, that like its eukaryotic relative forms protein filaments
in the presence of GTP. Since the discovery of the Z-ring 25 years ago, various
models for the role of FtsZ have been suggested. However, important information
about the architecture and dynamics of FtsZ filaments during cytokinesis is still
missing. One reason for this lack of knowledge has been the small size of bacteria,
which has made it difficult to resolve the orientation and dynamics of individual
FtsZ filaments in the Z-ring. While superresolution microscopy experiments have
helped to gain more information about the organization of the Z-ring in the dividing
cell, they were not yet able to elucidate a mechanism of how FtsZ filaments reorganize
during assembly and disassembly of the Z-ring. In this chapter, we explain how
to use an in vitro reconstitution approach to investigate the self-organization
of FtsZ filaments recruited to a biomimetic lipid bilayer by its membrane anchor
FtsA. We show how to perform single-molecule experiments to study the behavior
of individual FtsZ monomers during the constant reorganization of the FtsZ-FtsA
filament network. We describe how to analyze the dynamics of single molecules
and explain why this information can help to shed light onto possible mechanism
of Z-ring constriction. We believe that similar experimental approaches will be
useful to study the mechanism of membrane-based polymerization of other cytoskeletal
systems, not only from prokaryotic but also eukaryotic origin.
acknowledged_ssus:
- _id: Bio
acknowledgement: Natalia Baranova is supported by an EMBO Long-Term Fellowship (EMBO
ALTF 1163-2015) and Martin Loose by an ERC Starting Grant (ERCStG-2015-SelfOrganiCell).
alternative_title:
- Methods in Cell Biology
article_processing_charge: No
author:
- first_name: Natalia
full_name: Baranova, Natalia
id: 38661662-F248-11E8-B48F-1D18A9856A87
last_name: Baranova
orcid: 0000-0002-3086-9124
- first_name: Martin
full_name: Loose, Martin
id: 462D4284-F248-11E8-B48F-1D18A9856A87
last_name: Loose
orcid: 0000-0001-7309-9724
citation:
ama: 'Baranova NS, Loose M. Single-molecule measurements to study polymerization
dynamics of FtsZ-FtsA copolymers. In: Echard A, ed. Cytokinesis. Vol 137.
Academic Press; 2017:355-370. doi:10.1016/bs.mcb.2016.03.036'
apa: Baranova, N. S., & Loose, M. (2017). Single-molecule measurements to study
polymerization dynamics of FtsZ-FtsA copolymers. In A. Echard (Ed.), Cytokinesis
(Vol. 137, pp. 355–370). Academic Press. https://doi.org/10.1016/bs.mcb.2016.03.036
chicago: Baranova, Natalia S., and Martin Loose. “Single-Molecule Measurements to
Study Polymerization Dynamics of FtsZ-FtsA Copolymers.” In Cytokinesis,
edited by Arnaud Echard, 137:355–70. Academic Press, 2017. https://doi.org/10.1016/bs.mcb.2016.03.036.
ieee: N. S. Baranova and M. Loose, “Single-molecule measurements to study polymerization
dynamics of FtsZ-FtsA copolymers,” in Cytokinesis, vol. 137, A. Echard,
Ed. Academic Press, 2017, pp. 355–370.
ista: 'Baranova NS, Loose M. 2017.Single-molecule measurements to study polymerization
dynamics of FtsZ-FtsA copolymers. In: Cytokinesis. Methods in Cell Biology, vol.
137, 355–370.'
mla: Baranova, Natalia S., and Martin Loose. “Single-Molecule Measurements to Study
Polymerization Dynamics of FtsZ-FtsA Copolymers.” Cytokinesis, edited by
Arnaud Echard, vol. 137, Academic Press, 2017, pp. 355–70, doi:10.1016/bs.mcb.2016.03.036.
short: N.S. Baranova, M. Loose, in:, A. Echard (Ed.), Cytokinesis, Academic Press,
2017, pp. 355–370.
date_created: 2018-12-11T11:50:45Z
date_published: 2017-12-01T00:00:00Z
date_updated: 2023-09-20T11:16:30Z
day: '01'
department:
- _id: MaLo
doi: 10.1016/bs.mcb.2016.03.036
ec_funded: 1
editor:
- first_name: 'Arnaud '
full_name: 'Echard, Arnaud '
last_name: Echard
external_id:
isi:
- '000403542900022'
intvolume: ' 137'
isi: 1
language:
- iso: eng
month: '12'
oa_version: None
page: 355 - 370
project:
- _id: 2596EAB6-B435-11E9-9278-68D0E5697425
grant_number: ALTF 2015-1163
name: Synthesis of bacterial cell wall
- _id: 25681D80-B435-11E9-9278-68D0E5697425
call_identifier: FP7
grant_number: '291734'
name: International IST Postdoc Fellowship Programme
publication: Cytokinesis
publication_identifier:
issn:
- 0091679X
publication_status: published
publisher: Academic Press
publist_id: '6134'
quality_controlled: '1'
scopus_import: '1'
status: public
title: Single-molecule measurements to study polymerization dynamics of FtsZ-FtsA
copolymers
type: book_chapter
user_id: c635000d-4b10-11ee-a964-aac5a93f6ac1
volume: 137
year: '2017'
...