Watching helical membrane proteins fold reveals a common N-to-C-terminal folding pathway.
Science
; 366(6469): 1150-1156, 2019 11 29.
Article
in En
| MEDLINE
| ID: mdl-31780561
ABSTRACT
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 ß2-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.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Endopeptidases
/
Protein Folding
/
Receptors, Adrenergic, beta-2
/
Escherichia coli Proteins
/
DNA-Binding Proteins
/
Membrane Proteins
Limits:
Humans
Language:
En
Journal:
Science
Year:
2019
Type:
Article
Affiliation country:
South Korea