Format

Send to

Choose Destination
Proc Natl Acad Sci U S A. 2013 Sep 3;110(36):14640-5. doi: 10.1073/pnas.1306787110. Epub 2013 Aug 19.

Cotranslational folding of membrane proteins probed by arrest-peptide-mediated force measurements.

Author information

1
Center for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden.

Abstract

Polytopic membrane proteins are inserted cotranslationally into target membranes by ribosome-translocon complexes. It is, however, unclear when during the insertion process specific interactions between the transmembrane helices start to form. Here, we use a recently developed in vivo technique to measure pulling forces acting on transmembrane helices during their cotranslational insertion into the inner membrane of Escherichia coli to study the earliest steps of tertiary folding of five polytopic membrane proteins. We find that interactions between residues in a C-terminally located transmembrane helix and in more N-terminally located helices can be detected already at the point when the C-terminal helix partitions from the translocon into the membrane. Our findings pinpoint the earliest steps of tertiary structure formation and open up possibilities to study the cotranslational folding of polytopic membrane proteins.

KEYWORDS:

helix-helix interactions; membrane insertion; protein folding

PMID:
23959879
PMCID:
PMC3767533
DOI:
10.1073/pnas.1306787110
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for HighWire Icon for PubMed Central
Loading ...
Support Center