Autoren:	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
Titel:	IM30 IDPs form a membrane-protective carpet upon super-complex disassembly
Online-Publikationsdatum:	23-Apr-2021
Erscheinungsdatum:	2020
Sprache des Dokuments:	Englisch
Zusammenfassung/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-Sachgruppe:	540 Chemie 540 Chemistry and allied sciences 570 Biowissenschaften 570 Life sciences
Veröffentlichende Institution:	Johannes Gutenberg-Universität Mainz
Organisationseinheit:	FB 09 Chemie, Pharmazie u. Geowissensch. FB 08 Physik, Mathematik u. Informatik FB 10 Biologie
Veröffentlichungsort:	Mainz
ROR:	https://ror.org/023b0x485
DOI:	http://doi.org/10.25358/openscience-5762
Version:	Published version
Publikationstyp:	Zeitschriftenaufsatz
Nutzungsrechte:	CC BY
Informationen zu den Nutzungsrechten:	https://creativecommons.org/licenses/by/4.0/
Zeitschrift:	Communications biology 3
Seitenzahl oder Artikelnummer:	595
Verlag:	Springer Nature
Verlagsort:	London
Erscheinungsdatum:	2020
ISSN:	2399-3642
URL der Originalveröffentlichung:	https://doi.org/10.1038/s42003-020-01314-4
DOI der Originalveröffentlichung:	10.1038/s42003-020-01314-4
Enthalten in den Sammlungen:	JGU-Publikationen