Early encounters of a nascent membrane protein : specificity and timing of contacts inside and outside the ribosome

E.N.G. Houben, R. Zarivach, J Brunner, B. Oudega, S. Luirink

Research output: Contribution to JournalArticleAcademicpeer-review

Abstract

An unbiased photo-cross-linking approach was used to probe the "molecular path" of a growing nascent Escherichia coli inner membrane protein (IMP) from the peptidyl transferase center to the surface of the ribosome. The nascent chain was initially in proximity to the ribosomal proteins L4 and L22 and subsequently contacted L23, which is indicative of progression through the ribosome via the main ribosomal tunnel. The signal recognition particle (SRP) started to interact with the nascent IMP and to target the ribosome-nascent chain complex to the Sec-YidC complex in the inner membrane when maximally half of the transmembrane domain (TM) was exposed from the ribosomal exit. The combined data suggest a flexible tunnel that may accommodate partially folded nascent proteins and parts of the SRP and SecY. Intraribosomal contacts of the nascent chain were not influenced by the presence of a functional TM in the ribosome. © The Rockefeller University Press.
Original languageEnglish
Pages (from-to)27-35
Number of pages9
JournalJournal of Cell Biology
Volume170
DOIs
Publication statusPublished - 2005

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Ribosomes
Membrane Proteins
Signal Recognition Particle
Peptidyl Transferases
Molecular Probes
Escherichia coli
Membranes
Proteins

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abstract = "An unbiased photo-cross-linking approach was used to probe the {"}molecular path{"} of a growing nascent Escherichia coli inner membrane protein (IMP) from the peptidyl transferase center to the surface of the ribosome. The nascent chain was initially in proximity to the ribosomal proteins L4 and L22 and subsequently contacted L23, which is indicative of progression through the ribosome via the main ribosomal tunnel. The signal recognition particle (SRP) started to interact with the nascent IMP and to target the ribosome-nascent chain complex to the Sec-YidC complex in the inner membrane when maximally half of the transmembrane domain (TM) was exposed from the ribosomal exit. The combined data suggest a flexible tunnel that may accommodate partially folded nascent proteins and parts of the SRP and SecY. Intraribosomal contacts of the nascent chain were not influenced by the presence of a functional TM in the ribosome. {\circledC} The Rockefeller University Press.",
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Early encounters of a nascent membrane protein : specificity and timing of contacts inside and outside the ribosome. / Houben, E.N.G.; Zarivach, R.; Brunner, J; Oudega, B.; Luirink, S.

In: Journal of Cell Biology, Vol. 170, 2005, p. 27-35.

Research output: Contribution to JournalArticleAcademicpeer-review

TY - JOUR

T1 - Early encounters of a nascent membrane protein : specificity and timing of contacts inside and outside the ribosome

AU - Houben, E.N.G.

AU - Zarivach, R.

AU - Brunner, J

AU - Oudega, B.

AU - Luirink, S.

PY - 2005

Y1 - 2005

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AB - An unbiased photo-cross-linking approach was used to probe the "molecular path" of a growing nascent Escherichia coli inner membrane protein (IMP) from the peptidyl transferase center to the surface of the ribosome. The nascent chain was initially in proximity to the ribosomal proteins L4 and L22 and subsequently contacted L23, which is indicative of progression through the ribosome via the main ribosomal tunnel. The signal recognition particle (SRP) started to interact with the nascent IMP and to target the ribosome-nascent chain complex to the Sec-YidC complex in the inner membrane when maximally half of the transmembrane domain (TM) was exposed from the ribosomal exit. The combined data suggest a flexible tunnel that may accommodate partially folded nascent proteins and parts of the SRP and SecY. Intraribosomal contacts of the nascent chain were not influenced by the presence of a functional TM in the ribosome. © The Rockefeller University Press.

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