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Biological insights from a simulation model of the critical FtsZ accumulation required for prokaryotic cell division
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Dow, Claire E., Berg, Hugo van den, Roper, David I. and Rodger, Alison (2015) Biological insights from a simulation model of the critical FtsZ accumulation required for prokaryotic cell division. Biochemistry, 54 (24). pp. 3803-3813. doi:10.1021/acs.biochem.5b00261 ISSN 0006-2960.
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Official URL: http://dx.doi.org/10.1021/acs.biochem.5b00261
Abstract
A simulation model of prokaryotic Z-ring assembly, based on the observed behavior of FtsZ in vitro as well as on in vivo parameters, is used to integrate critical processes in cell division. According to the model, the cell’s ability to divide depends on a “contraction parameter” (χ) that links the force of contraction to the dynamics of FtsZ. This parameter accurately predicts the outcome of division. Evaluating the GTP binding strength, the FtsZ polymerization rate, and the intrinsic GTP hydrolysis/dissociation activity, we find that inhibition of GTP–FtsZ binding is an inefficient antibacterial target. Furthermore, simulations indicate that the temperature sensitivity of the ftsZ84 mutation arises from the conversion of FtsZ to a dual-specificity NTPase. Finally, the sensitivity to temperature of the rate of ATP hydrolysis, over the critical temperature range, leads us to conclude that the ftsZ84 mutation affects the turnover rate of the Z-ring much less strongly than previously reported.
Item Type: | Journal Article | ||||||||
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Subjects: | Q Science > QA Mathematics Q Science > QR Microbiology |
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Divisions: | Faculty of Science, Engineering and Medicine > Science > Chemistry Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) Faculty of Science, Engineering and Medicine > Science > Mathematics |
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Library of Congress Subject Headings (LCSH): | Prokaryotes, Cell division -- Mathematical models | ||||||||
Journal or Publication Title: | Biochemistry | ||||||||
Publisher: | American Chemical Society | ||||||||
ISSN: | 0006-2960 | ||||||||
Official Date: | 1 June 2015 | ||||||||
Dates: |
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Volume: | 54 | ||||||||
Number: | 24 | ||||||||
Page Range: | pp. 3803-3813 | ||||||||
DOI: | 10.1021/acs.biochem.5b00261 | ||||||||
Status: | Peer Reviewed | ||||||||
Publication Status: | Published | ||||||||
Access rights to Published version: | Restricted or Subscription Access | ||||||||
Date of first compliant deposit: | 29 December 2015 | ||||||||
Date of first compliant Open Access: | 27 June 2016 | ||||||||
Funder: | Engineering and Physical Sciences Research Council (EPSRC) | ||||||||
Grant number: | EP/F500378/1 (EPSRC) | ||||||||
Adapted As: |
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