Lipid-polymer nanoparticles to probe the native-like environment of intramembrane rhomboid protease GlpG and its activity

Henry Sawczyc, Takashi Tatsuta, Carl Öster, Spyridon Kosteletos, Sascha Lange, Claudia Bohg, Thomas Langer and Adam Lange ()
Additional contact information
Henry Sawczyc: Leibniz-Forschungsinstitut für Molekulare Pharmakologie
Takashi Tatsuta: Department of Mitochondrial Proteostasis
Carl Öster: Leibniz-Forschungsinstitut für Molekulare Pharmakologie
Spyridon Kosteletos: Leibniz-Forschungsinstitut für Molekulare Pharmakologie
Sascha Lange: Leibniz-Forschungsinstitut für Molekulare Pharmakologie
Claudia Bohg: Leibniz-Forschungsinstitut für Molekulare Pharmakologie
Thomas Langer: Department of Mitochondrial Proteostasis
Adam Lange: Leibniz-Forschungsinstitut für Molekulare Pharmakologie

Nature Communications, 2024, vol. 15, issue 1, 1-9

Abstract: Abstract Polymers can facilitate detergent-free extraction of membrane proteins into nanodiscs (e.g., SMALPs, DIBMALPs), incorporating both integral membrane proteins as well as co-extracted native membrane lipids. Lipid-only SMALPs and DIBMALPs have been shown to possess a unique property; the ability to exchange lipids through ‘collisional lipid mixing’. Here we expand upon this mixing to include protein-containing DIBMALPs, using the rhomboid protease GlpG. Through lipidomic analysis before and after incubation with DMPC or POPC DIBMALPs, we show that lipids are rapidly exchanged between protein and lipid-only DIBMALPs, and can be used to identify bound or associated lipids through ‘washing-in’ exogenous lipids. Additionally, through the requirement of rhomboid proteases to cleave intramembrane substrates, we show that this mixing can be performed for two protein-containing DIBMALP populations, assessing the native function of intramembrane proteolysis and demonstrating that this mixing has no deleterious effects on protein stability or structure.

Date: 2024
References: View references in EconPapers View complete reference list from CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/s41467-024-51989-0 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-51989-0

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-024-51989-0

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().