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
Year of first publication:	2020
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