Please use this identifier to cite or link to this item: http://doi.org/10.25358/openscience-8174
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dc.contributor.authorAhlswede, Lena-
dc.contributor.authorSiebenaller, Carmen-
dc.contributor.authorJunglas, Benedikt-
dc.contributor.authorHellmann, Nadja-
dc.contributor.authorSchneider, Dirk-
dc.date.accessioned2022-10-26T10:17:03Z-
dc.date.available2022-10-26T10:17:03Z-
dc.date.issued2022-
dc.identifier.urihttps://openscience.ub.uni-mainz.de/handle/20.500.12030/8189-
dc.description.abstractHuman Claudin-7 (Cldn7) is a member of the Claudin (Cldn) superfamily. In vivo, these proteins form tight junctions, which establish constricted connections between cells. Cldns oligomerize within the membrane plane (= cis-interaction), and also interact with Cldns from adjacent cells (= trans-interaction). Interactions of Cldns are typically studied in vivo and structural analyses of isolated Cldns are limited. Here, we describe heterologous expression in E. coli and purification of human Cldn7, enabling in vitro analyses of the isolated protein using detergent and model membrane systems. Cldn7 exists as a monomer, hexamer, and various higher oligomers in micelles. While only limited unfolding of the protein was observed in the presence of the anionic detergent sodium dodecyl sulfate, decreased ionic strength did affect Cldn7 cis-interactions. Furthermore, we identified two amino acids which mediate electrostatic cis-interactions and analyzed the impact of disturbed cis-interaction on trans-contacts via atomic force microscopy and monitoring Förster resonance energy transfer between fluorescently labeled Cldn7-containing proteoliposomes. Our results indicate that Cldn7 cis-oligomerization might not be a prerequisite for establishing trans-contacts.en_GB
dc.description.sponsorshipGefördert durch die Deutsche Forschungsgemeinschaft (DFG) - Projektnummer 491381577de
dc.language.isoengde
dc.rightsCC BY*
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/*
dc.subject.ddc570 Biowissenschaftende_DE
dc.subject.ddc570 Life sciencesen_GB
dc.titleHuman Claudin-7 cis-interactions are not crucial for membrane-membrane (trans-) interactionsen_GB
dc.typeZeitschriftenaufsatzde
dc.identifier.doihttp://doi.org/10.25358/openscience-8174-
jgu.type.contenttypeScientific articlede
jgu.type.dinitypearticleen_GB
jgu.type.versionPublished versionde
jgu.type.resourceTextde
jgu.organisation.departmentFB 09 Chemie, Pharmazie u. Geowissensch.de
jgu.organisation.number7950-
jgu.organisation.nameJohannes Gutenberg-Universität Mainz-
jgu.rights.accessrightsopenAccess-
jgu.journal.titleFrontiers in molecular biosciencesde
jgu.journal.volume9de
jgu.pages.alternative908383de
jgu.publisher.year2022-
jgu.publisher.nameFrontiers Mediade
jgu.publisher.placeLausannede
jgu.publisher.urihttps://doi.org/10.3389/fmolb.2022.908383de
jgu.publisher.issn2296-889Xde
jgu.organisation.placeMainz-
jgu.subject.ddccode570de
jgu.publisher.doi10.3389/fmolb.2022.908383de
jgu.organisation.rorhttps://ror.org/023b0x485-
jgu.subject.dfgNaturwissenschaftende
Appears in collections:DFG-491381577-G

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