Polytopic membrane protein folding at L17 in the ribosome tunnel initiates cyclical changes at the translocon

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Polytopic membrane protein folding at L17 in the ribosome tunnel initiates cyclical changes at the translocon

Multi-spanning membrane protein loops are directed alternately into the cytosol or ER lumen during cotranslational integration. Nascent chain exposure is switched after a newly synthesized transmembrane segment (TMS) enters the ribosomal tunnel. FRET measurements revealed that each TMS is initially extended, but folds into a compact conformation after moving 6-7 residues from the peptidyltransf...

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Polytopic membrane protein folding at L 17 in the ribosome tunnel initiates cyclical

The Rockefeller University Press $30.00 J. Cell Biol. Vol. 195 No. 1 55–70 www.jcb.org/cgi/doi/10.1083/jcb.201103118 JCB 55 Correspondence to Arthur E. Johnson: [email protected] Abbreviations used in this paper: A, acceptor-containing sample; B, sample lacking acceptor and donor; D, donor-containing sample; DA, sample containing donor and acceptor; Ac-Lys, N-acetyl-lysine; ANB-Ly...

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Cotranslational Protein Folding inside the Ribosome Exit Tunnel

At what point during translation do proteins fold? It is well established that proteins can fold cotranslationally outside the ribosome exit tunnel, whereas studies of folding inside the exit tunnel have so far detected only the formation of helical secondary structure and collapsed or partially structured folding intermediates. Here, using a combination of cotranslational nascent chain force m...

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Why a protein switches sides during translation

M ultipass transmembrane proteins weave back and forth across the lipid bilayer. Two papers by Lin et al. (1, 2) reveal that information encoded within the proteins helps defi ne this alternating pattern. A protein destined for the plasma membrane usually starts out in the ER. As translation of the protein’s mRNA begins, the newly made polypeptide slips into the ER membrane. As the protein elon...

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Protein folding on the ribosome.

In living systems, polypeptide chains are synthesised on ribosomes, molecular machines composed of over 50 protein and nucleic acid molecules. As nascent chains emerge from the ribosomal exit tunnel and into the cellular environment, the majority must fold into specific structures in order to function. In this article we discuss recent approaches designed to reveal how such folding occurs and r...

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ژورنال

عنوان ژورنال: Journal of Cell Biology

سال: 2011

ISSN: 1540-8140,0021-9525

DOI: 10.1083/jcb.201103118