Please use this identifier to cite or link to this item: http://doi.org/10.25358/openscience-5762
Authors: Junglas, Benedikt
Orru, Roberto
Axt, Amelie
Siebenaller, Carmen
Steinchen, Wieland
Heidrich, Jennifer
Hellmich, Ute A.
Hellmann, Nadja
Wolf, Eva
Weber, Stefan A. L.
Schneider, Dirk
Title: IM30 IDPs form a membrane-protective carpet upon super-complex disassembly
Online publication date: 23-Apr-2021
Language: english
Abstract: Members 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.
DDC: 540 Chemie
540 Chemistry and allied sciences
570 Biowissenschaften
570 Life sciences
Institution: Johannes Gutenberg-Universität Mainz
Department: FB 09 Chemie, Pharmazie u. Geowissensch.
FB 08 Physik, Mathematik u. Informatik
FB 10 Biologie
Place: Mainz
ROR: https://ror.org/023b0x485
DOI: http://doi.org/10.25358/openscience-5762
Version: Published version
Publication type: Zeitschriftenaufsatz
License: CC BY
Information on rights of use: https://creativecommons.org/licenses/by/4.0/
Journal: Communications biology
3
Pages or article number: 595
Publisher: Springer Nature
Publisher place: London
Issue date: 2020
ISSN: 2399-3642
Publisher URL: https://doi.org/10.1038/s42003-020-01314-4
Publisher DOI: 10.1038/s42003-020-01314-4
Appears in collections:JGU-Publikationen

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