Watching helical membrane proteins fold reveals a common N-to-C-terminal folding pathway

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To understand membrane protein biogenesis, we need to explore folding within a bilayer context. Here, we describe a single-molecule force microscopy technique that monitors the folding of helical membrane proteins in vesicle and bicelle environments. After completely unfolding the protein at high force, we lower the force to initiate folding while transmembrane helices are aligned in a zigzag manner within the bilayer, thereby imposing minimal constraints on folding. We used the approach to characterize the folding pathways of the Escherichia coli rhomboid protease GlpG and the human beta(2)-adrenergic receptor. Despite their evolutionary distance, both proteins fold in a strict N-to-C-terminal fashion, accruing structures in units of helical hairpins. These common features suggest that integral helical membrane proteins have evolved to maximize their fitness with cotranslational folding.
Publisher
AMER ASSOC ADVANCEMENT SCIENCE
Issue Date
2019-11
Language
English
Article Type
Article
Citation

SCIENCE, v.366, no.6469, pp.1150 - +

ISSN
0036-8075
DOI
10.1126/science.aaw8208
URI
http://hdl.handle.net/10203/270287
Appears in Collection
PH-Journal Papers(저널논문)
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