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

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.

SUBMITTER: Cymer F

PROVIDER: S-EPMC3767533 | biostudies-literature | 2013 Sep

REPOSITORIES: biostudies-literature

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

Cymer Florian F von Heijne Gunnar G

Proceedings of the National Academy of Sciences of the United States of America 20130819 36

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 polytop ...[more]

PMID: 23959879

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