Computational modeling of unphosphorylated CtrA:Cori binding in the Caulobacter cell cycle

Summary: In the alphaproteobacterium, Caulobacter crescentus, phosphorylated CtrA (CtrA∼P), a master regulatory protein, binds directly to the chromosome origin (Cori) to inhibit DNA replication. Using a mathematical model of CtrA binding at Cori site [d], we provide computational evidence that CtrA...

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Autores principales:	Bronson R. Weston, John J. Tyson, Yang Cao
Formato:	article
Lenguaje:	EN
Publicado:	Elsevier 2021
Materias:	Bacteriology In silico biology Mathematical biosciences Science Q
Acceso en línea:	https://doaj.org/article/c84aecc762214e299ba19b6016248efd
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spelling	oai:doaj.org-article:c84aecc762214e299ba19b6016248efd2021-12-02T05:03:30ZComputational modeling of unphosphorylated CtrA:Cori binding in the Caulobacter cell cycle2589-004210.1016/j.isci.2021.103413https://doaj.org/article/c84aecc762214e299ba19b6016248efd2021-12-01T00:00:00Zhttp://www.sciencedirect.com/science/article/pii/S2589004221013845https://doaj.org/toc/2589-0042Summary: In the alphaproteobacterium, Caulobacter crescentus, phosphorylated CtrA (CtrA∼P), a master regulatory protein, binds directly to the chromosome origin (Cori) to inhibit DNA replication. Using a mathematical model of CtrA binding at Cori site [d], we provide computational evidence that CtrAU can displace CtrA∼P from Cori at the G1-S transition. Investigation of this interaction within a detailed model of the C. crescentus cell cycle suggests that CckA phosphatase may clear Cori of CtrA∼P by altering the [CtrAU]/[CtrA∼P] ratio rather than by completely depleting CtrA∼P. Model analysis reveals that the mechanism allows for a speedier transition into S phase, stabilizes the timing of chromosome replication under fluctuating rates of CtrA proteolysis, and may contribute to the viability of numerous mutant strains. Overall, these results suggest that CtrAU enhances the robustness of chromosome replication. More generally, our proposed regulation of CtrA:Cori dynamics may represent a novel motif for molecular signaling in cell physiology.Bronson R. WestonJohn J. TysonYang CaoElsevierarticleBacteriologyIn silico biologyMathematical biosciencesScienceQENiScience, Vol 24, Iss 12, Pp 103413- (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Bacteriology In silico biology Mathematical biosciences Science Q
spellingShingle	Bacteriology In silico biology Mathematical biosciences Science Q Bronson R. Weston John J. Tyson Yang Cao Computational modeling of unphosphorylated CtrA:Cori binding in the Caulobacter cell cycle
description	Summary: In the alphaproteobacterium, Caulobacter crescentus, phosphorylated CtrA (CtrA∼P), a master regulatory protein, binds directly to the chromosome origin (Cori) to inhibit DNA replication. Using a mathematical model of CtrA binding at Cori site [d], we provide computational evidence that CtrAU can displace CtrA∼P from Cori at the G1-S transition. Investigation of this interaction within a detailed model of the C. crescentus cell cycle suggests that CckA phosphatase may clear Cori of CtrA∼P by altering the [CtrAU]/[CtrA∼P] ratio rather than by completely depleting CtrA∼P. Model analysis reveals that the mechanism allows for a speedier transition into S phase, stabilizes the timing of chromosome replication under fluctuating rates of CtrA proteolysis, and may contribute to the viability of numerous mutant strains. Overall, these results suggest that CtrAU enhances the robustness of chromosome replication. More generally, our proposed regulation of CtrA:Cori dynamics may represent a novel motif for molecular signaling in cell physiology.
format	article
author	Bronson R. Weston John J. Tyson Yang Cao
author_facet	Bronson R. Weston John J. Tyson Yang Cao
author_sort	Bronson R. Weston
title	Computational modeling of unphosphorylated CtrA:Cori binding in the Caulobacter cell cycle
title_short	Computational modeling of unphosphorylated CtrA:Cori binding in the Caulobacter cell cycle
title_full	Computational modeling of unphosphorylated CtrA:Cori binding in the Caulobacter cell cycle
title_fullStr	Computational modeling of unphosphorylated CtrA:Cori binding in the Caulobacter cell cycle
title_full_unstemmed	Computational modeling of unphosphorylated CtrA:Cori binding in the Caulobacter cell cycle
title_sort	computational modeling of unphosphorylated ctra:cori binding in the caulobacter cell cycle
publisher	Elsevier
publishDate	2021
url	https://doaj.org/article/c84aecc762214e299ba19b6016248efd
work_keys_str_mv	AT bronsonrweston computationalmodelingofunphosphorylatedctracoribindinginthecaulobactercellcycle AT johnjtyson computationalmodelingofunphosphorylatedctracoribindinginthecaulobactercellcycle AT yangcao computationalmodelingofunphosphorylatedctracoribindinginthecaulobactercellcycle
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Computational modeling of unphosphorylated CtrA:Cori binding in the Caulobacter cell cycle

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