IM30 IDPs form a membrane-protective carpet upon super-complex disassembly

dc.contributor.authorJunglas, Benedikt
dc.contributor.authorOrru, Roberto
dc.contributor.authorAxt, Amelie
dc.contributor.authorSiebenaller, Carmen
dc.contributor.authorSteinchen, Wieland
dc.contributor.authorHeidrich, Jennifer
dc.contributor.authorHellmich, Ute A.
dc.contributor.authorHellmann, Nadja
dc.contributor.authorWolf, Eva
dc.contributor.authorWeber, Stefan A. L.
dc.contributor.authorSchneider, Dirk
dc.date.accessioned2021-04-23T08:50:35Z
dc.date.available2021-04-23T08:50:35Z
dc.date.issued2020
dc.description.abstractMembers of the phage shock protein A (PspA) family, including the inner membrane-associated protein of 30 kDa (IM30), are suggested to stabilize stressed cellular membranes. Furthermore, IM30 is essential in thylakoid membrane-containing chloroplasts and cyanobacteria, where it is involved in membrane biogenesis and/or remodeling. While it is well known that PspA and IM30 bind to membranes, the mechanism of membrane stabilization is still enigmatic. Here we report that ring-shaped IM30 super-complexes disassemble on membranes, resulting in formation of a membrane-protecting protein carpet. Upon ring dissociation, the C-terminal domain of IM30 unfolds, and the protomers self-assemble on membranes. IM30 assemblies at membranes have been observed before in vivo and were associated with stress response in cyanobacteria and chloroplasts. These assemblies likely correspond to the here identified carpet structures. Our study defines the thus far enigmatic structural basis for the physiological function of IM30 and related proteins, including PspA, and highlights a hitherto unrecognized concept of membrane stabilization by intrinsically disordered proteins.en_GB
dc.identifier.doihttp://doi.org/10.25358/openscience-5762
dc.identifier.urihttps://openscience.ub.uni-mainz.de/handle/20.500.12030/5771
dc.language.isoengde
dc.rightsCC-BY-4.0*
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/*
dc.subject.ddc540 Chemiede_DE
dc.subject.ddc540 Chemistry and allied sciencesen_GB
dc.subject.ddc570 Biowissenschaftende_DE
dc.subject.ddc570 Life sciencesen_GB
dc.titleIM30 IDPs form a membrane-protective carpet upon super-complex disassemblyen_GB
dc.typeZeitschriftenaufsatzde
jgu.journal.titleCommunications biologyde
jgu.journal.volume3de
jgu.organisation.departmentFB 09 Chemie, Pharmazie u. Geowissensch.de
jgu.organisation.departmentFB 08 Physik, Mathematik u. Informatik
jgu.organisation.departmentFB 10 Biologie
jgu.organisation.nameJohannes Gutenberg-Universität Mainz
jgu.organisation.number7950
jgu.organisation.number7940
jgu.organisation.number7970
jgu.organisation.placeMainz
jgu.organisation.rorhttps://ror.org/023b0x485
jgu.pages.alternative595de
jgu.publisher.doi10.1038/s42003-020-01314-4
jgu.publisher.issn2399-3642de
jgu.publisher.nameSpringer Naturede
jgu.publisher.placeLondonde
jgu.publisher.urihttps://doi.org/10.1038/s42003-020-01314-4de
jgu.publisher.year2020
jgu.rights.accessrightsopenAccess
jgu.subject.ddccode540de
jgu.subject.ddccode570de
jgu.type.dinitypeArticleen_GB
jgu.type.resourceTextde
jgu.type.versionPublished versionde

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