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dc.contributor.authorVaknin, Ady
dc.contributor.authorBerg, Howard
dc.date.accessioned2019-10-11T12:28:47Z
dc.date.issued2006
dc.identifier.citationVaknin, A., and H. C. Berg. 2006. “Osmotic Stress Mechanically Perturbs Chemoreceptors in Escherichia Coli.” Proceedings of the National Academy of Sciences103 (3): 592–96. https://doi.org/10.1073/pnas.0510047103.
dc.identifier.issn0027-8424
dc.identifier.issn0744-2831
dc.identifier.issn1091-6490
dc.identifier.urihttp://nrs.harvard.edu/urn-3:HUL.InstRepos:41534327*
dc.description.abstractTwo-component signaling systems play a major role in the long-term adaptation of microorganisms to changes in osmolarity, but how osmoreceptors work is not well understood. Temporal changes in solute concentration are sensed by the chemotaxis system in Escherichia coli, enabling these bacteria to avoid regions of high osmolarity. To study how osmolarity is detected in this system, we fused yellow fluorescent protein (YFP) to the C terminus of the serine or aspartate chemoreceptor, monitored the steady-state fluorescence polarization of YFP, and found that the polarization decreased substantially upon addition of osmotic agents. This decrease was due to an increase in fluorescence resonance energy transfer between YFP fluorophores in adjacent homodimers within trimers of dimers. Thus, changes in homodimer spacing and/or orientation appear to initiate osmotactic signaling.
dc.language.isoen_US
dc.publisherNational Academy of Sciences
dash.licenseLAA
dc.titleOsmotic stress mechanically perturbs chemoreceptors in Escherichia coli
dc.typeJournal Article
dc.description.versionVersion of Record
dc.relation.journalProceedings of the National Academy of Sciences of the United States of America
dash.depositing.authorBerg, Howard Curtis::246ef0f2a815e6b01ad2b2628664c858::600
dc.date.available2019-10-11T12:28:47Z
dash.workflow.comments1Science Serial ID 89961
dc.identifier.doi10.1073/pnas.0510047103
dash.source.volume103;3
dash.source.page592


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