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  • Öjemalm, KarinStockholms universitet,Institutionen för biokemi och biofysik (author)

Apolar surface area determines the efficiency of translocon-mediated membrane-protein integration into the endoplasmic reticulum

  • Article/chapterEnglish2011

Publisher, publication year, extent ...

  • 2011-05-23
  • Proceedings of the National Academy of Sciences,2011
  • printrdacarrier

Numbers

  • LIBRIS-ID:oai:DiVA.org:su-71400
  • https://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-71400URI
  • https://doi.org/10.1073/pnas.1100120108DOI

Supplementary language notes

  • Language:English
  • Summary in:English

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  • Subject category:ref swepub-contenttype
  • Subject category:art swepub-publicationtype

Notes

  • Integral membrane proteins are integrated cotranslationally into the membrane of the endoplasmic reticulum in a process mediated by the Sec61 translocon. Transmembrane α-helices in a translocating polypeptide chain gain access to the surrounding membrane through a lateral gate in the wall of the translocon channel [van den Berg B, et al. (2004) Nature427:36–44; Zimmer J, et al. (2008) Nature455:936–943; Egea PF, Stroud RM (2010)Proc Natl Acad Sci USA 107:17182–17187]. To clarify the nature of the membrane-integration process, we have measured the insertion efficiency into the endoplasmic reticulum membrane of model hydrophobic segments containing nonproteinogenic aliphatic and aromatic amino acids. We find that an amino acid’s contribution to the apparent free energy of membrane-insertion is directly proportional to the nonpolar accessible surface area of its side chain, as expected for thermodynamic partitioning between aqueous and nonpolar phases. But unlike bulk-phase partitioning, characterized by a nonpolar solvation parameter of 23 cal∕ðmol · Å2Þ, the solvation parameter for transfer from translocon to bilayer is 6 –10 cal∕ðmol · Å2Þ, pointing to important differences between translocon-guided partitioning and simple water-to-membrane partitioning. Our results provide compelling evidence for a termodynamic partitioning model and insights into the physical properties of the translocon.

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Added entries (persons, corporate bodies, meetings, titles ...)

  • Higuchi, Takashi (author)
  • Jiang, YangStockholms universitet,Institutionen för neurokemi (author)
  • Langel, ÜloStockholms universitet,Institutionen för neurokemi(Swepub:su)ulo (author)
  • Nilsson, IngMarieStockholms universitet,Institutionen för biokemi och biofysik(Swepub:su)inils (author)
  • White, Stephen H. (author)
  • Suga, Hiroaki (author)
  • von Heijne, GunnarStockholms universitet,Institutionen för biokemi och biofysik,Science for Life Laboratory (SciLifeLab)(Swepub:su)heijn (author)
  • Stockholms universitetInstitutionen för biokemi och biofysik (creator_code:org_t)

Related titles

  • In:Proceedings of the National Academy of Sciences of the United States of America: Proceedings of the National Academy of Sciences108:31, s. E359-E3640027-84241091-6490

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