Biologically sound formal model of Hsp70 heat induction

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dc.contributor.authorDudziuk, Grzegorz
dc.contributor.authorWronowska, Weronika
dc.contributor.authorGambin, Anna
dc.contributor.authorSzymańska, Zuzanna
dc.contributor.authorRybiński, Mikołaj
dc.contributor.organizationInterdisciplinary Centre for Mathematical and Computational Modelling, University of Warsawen
dc.contributor.organizationCentre of New Technologies, University of Warsawen
dc.contributor.organizationFaculty of Biology, University of Warsawen
dc.contributor.organizationInstitute of Informatics, Faculty of Mathematics, Informatics and Mechanics, University of Warsawen
dc.contributor.organizationInstitute of Mathematics, Polish Academy of Sciencesen
dc.contributor.organizationDepartment of Biosystems, Science and Engineering, ETH Zurich, Basel, Switzerlanden
dc.date.accessioned2022-05-16T14:44:03Z
dc.date.available2022-05-16T14:44:03Z
dc.date.issued2019
dc.description.abstractA proper response to rapid environmental changes is essential for cell survival and requires efficient modifications in the pattern of gene expression. In this respect, a prominent example is Hsp70, a chaperone protein whose synthesis is dynamically regulated in stress conditions. In this paper, we expand a formal model of Hsp70 heat induction originally proposed in previous articles. To accurately capture various modes of heat shock effects, we not only introduce temperature dependencies in transcription to Hsp70 mRNA and in dissociation of transcriptional complexes, but we also derive a new formal expression for the temperature dependence in protein denaturation. We calibrate our model using comprehensive sets of both previously published experimental data and also biologically justified constraints. Interestingly, we obtain a biologically plausible temperature dependence of the transcriptional complex dissociation, despite the lack of biological constraints imposed in the calibration process. Finally, based on a sensitivity analysis of the model carried out in both deterministic and stochastic settings, we suggest that the regulation of the binding of transcriptional complexes plays a key role in Hsp70 induction upon heat shock. In conclusion, we provide a model that is able to capture the essential dynamics of the Hsp70 heat induction whilst being biologically sound in terms of temperature dependencies, description of protein denaturation and imposed calibration constraints.en
dc.identifier.citationWronowska, Weronika and Szymańska, Zuzanna and Gambin, Anna and Dudziuk, Grzegorz and Rybiński, Mikołaj Jakub."Biologically sound formal model of Hsp70 heat induction". Journal of Theoretical Biology (2019) 74-101 https://doi.org/10.1016/j.jtbi.2019.05.022en
dc.identifier.doi10.1016/j.jtbi.2019.05.022
dc.identifier.issn0022-5193
dc.identifier.urihttps://open.icm.edu.pl/handle/123456789/21282
dc.language.isoen
dc.publisherElsevieren
dc.rightsUznanie autorstwa 4.0 Międzynarodowe*
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/*
dc.subjectsystem biologyen
dc.subjectheat shock responseen
dc.subjectsensitivity analysisen
dc.subjectparameter estimationen
dc.subjectHsp70en
dc.titleBiologically sound formal model of Hsp70 heat inductionpl
dc.typearticleen
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