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Insertion of short transmembrane helices by the Sec61 translocon
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Jaud, Simon (författare)
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Fernández-Vidal, Mónica (författare)
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- Nilsson, IngMarie (författare)
- Stockholms universitet,Institutionen för biokemi och biofysik
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- Meindl-Beinker, Nadja M. (författare)
- Stockholms universitet,Institutionen för biokemi och biofysik
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- Hübner, Nadja C. (författare)
- Stockholms universitet,Institutionen för biokemi och biofysik
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Tobias, Douglas J. (författare)
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- von Heijne, Gunnar (författare)
- Stockholms universitet,Institutionen för biokemi och biofysik
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White, Stephen H. (författare)
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(creator_code:org_t)
- 2009-07-14
- Engelska.
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Ingår i: Proceedings of the National Academy of Sciences of the United States of America. - : Proceedings of the National Academy of Sciences. - 0027-8424 .- 1091-6490. ; 106:28, s. 11588-11593
- Relaterad länk:
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https://www.pnas.org...
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- The insertion efficiency of transmembrane (TM) helices by the Sec61 translocon depends on helix amino acid composition, the positions of the amino acids within the helix, and helix length. We have used an in vitro expression system to examine systematically the insertion efficiency of short polyleucine segments (L(n), n = 4 ... 12) flanked at either end by 4-residue sequences of the form XXPX-L(n)-XPXX with X = G, N, D, or K. Except for X = K, insertion efficiency (p) is <10% for n < 8, but rises steeply to 100% for n = 12. For X = K, p is already close to 100% for n = 10. A similar pattern is observed for synthetic peptides incorporated into oriented phospholipid bilayer arrays, consistent with the idea that recognition of TM segments by the translocon critically involves physical partitioning of nascent peptide chains into the lipid bilayer. Molecular dynamics simulations suggest that insertion efficiency is determined primarily by the energetic cost of distorting the bilayer in the vicinity of the TM helix. Very short lysine-flanked leucine segments can reduce the energetic cost by extensive hydrogen bonding with water and lipid phosphate groups (snorkeling) and by partial unfolding.
Ämnesord
- NATURVETENSKAP -- Biologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences (hsv//eng)
- NATURVETENSKAP -- Kemi (hsv//swe)
- NATURAL SCIENCES -- Chemical Sciences (hsv//eng)
Nyckelord
- hydrophobic mismatch
- membrane protein synthesis
- membrane proteins
- molecular dynamics simulation
- lipid bilayer
- NATURAL SCIENCES
- NATURVETENSKAP
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)