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dc.contributor.authorCuevas-Velazquez, Cesar L
dc.contributor.authorVellosillo, Tamara
dc.contributor.authorGuadalupe, Karina
dc.contributor.authorSchmidt, Hermann Broder
dc.contributor.authorYu, Feng
dc.contributor.authorMoses, David
dc.contributor.authorBrophy, Jennifer AN
dc.contributor.authorCosio-Acosta, Dante
dc.contributor.authorDas, Alakananda
dc.contributor.authorWang, Lingxin
dc.contributor.authorJones, Alexander
dc.contributor.authorCovarrubias, Alejandra A
dc.contributor.authorSukenik, Shahar
dc.contributor.authorDinneny, José R
dc.date.accessioned2021-11-23T00:30:18Z
dc.date.available2021-11-23T00:30:18Z
dc.date.issued2021-09-14
dc.identifier.issn2041-1723
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/330942
dc.description.abstractCell homeostasis is perturbed when dramatic shifts in the external environment cause the physical-chemical properties inside the cell to change. Experimental approaches for dynamically monitoring these intracellular effects are currently lacking. Here, we leverage the environmental sensitivity and structural plasticity of intrinsically disordered protein regions (IDRs) to develop a FRET biosensor capable of monitoring rapid intracellular changes caused by osmotic stress. The biosensor, named SED1, utilizes the Arabidopsis intrinsically disordered AtLEA4-5 protein expressed in plants under water deficit. Computational modeling and in vitro studies reveal that SED1 is highly sensitive to macromolecular crowding. SED1 exhibits large and near-linear osmolarity-dependent changes in FRET inside living bacteria, yeast, plant, and human cells, demonstrating the broad utility of this tool for studying water-associated stress. This study demonstrates the remarkable ability of IDRs to sense the cellular environment across the tree of life and provides a blueprint for their use as environmentally-responsive molecular tools.
dc.format.mediumElectronic
dc.languageeng
dc.publisherSpringer Science and Business Media LLC
dc.rightsAttribution 4.0 International
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.subjectCell Line, Tumor
dc.subjectOsteoblasts
dc.subjectHumans
dc.subjectEscherichia coli
dc.subjectSaccharomyces cerevisiae
dc.subjectArabidopsis
dc.subjectWater
dc.subjectMolecular Chaperones
dc.subjectArabidopsis Proteins
dc.subjectRecombinant Proteins
dc.subjectFluorescence Resonance Energy Transfer
dc.subjectBiosensing Techniques
dc.subjectGene Expression
dc.subjectBinding Sites
dc.subjectProtein Conformation
dc.subjectProtein Binding
dc.subjectKinetics
dc.subjectOsmolar Concentration
dc.subjectOsmotic Pressure
dc.subjectThermodynamics
dc.subjectModels, Molecular
dc.subjectProtein Interaction Domains and Motifs
dc.subjectIntrinsically Disordered Proteins
dc.titleIntrinsically disordered protein biosensor tracks the physical-chemical effects of osmotic stress on cells.
dc.typeArticle
prism.issueIdentifier1
prism.publicationDate2021
prism.publicationNameNat Commun
prism.startingPage5438
prism.volume12
dc.identifier.doi10.17863/CAM.78386
dcterms.dateAccepted2021-08-27
rioxxterms.versionofrecord10.1038/s41467-021-25736-8
rioxxterms.versionVoR
rioxxterms.licenseref.urihttp://www.rioxx.net/licenses/all-rights-reserved
rioxxterms.licenseref.startdate2021-09-14
dc.contributor.orcidCuevas-Velazquez, Cesar L [0000-0002-6629-6444]
dc.contributor.orcidSchmidt, Hermann Broder [0000-0002-0750-8419]
dc.contributor.orcidYu, Feng [0000-0003-1755-5515]
dc.contributor.orcidMoses, David [0000-0002-5189-5188]
dc.contributor.orcidJones, Alexander [0000-0002-3662-2915]
dc.contributor.orcidCovarrubias, Alejandra A [0000-0003-0439-3414]
dc.contributor.orcidSukenik, Shahar [0000-0003-3855-9574]
dc.contributor.orcidDinneny, José R [0000-0002-3998-724X]
dc.identifier.eissn2041-1723
rioxxterms.typeJournal Article/Review
cam.issuedOnline2021-09-14


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Attribution 4.0 International
Except where otherwise noted, this item's licence is described as Attribution 4.0 International