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Asn- and Asp-mediated interactions between transmembrane helices during translocon-mediated membrane protein assembly
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
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2006 (English)In: EMBO reports, ISSN 1469-221X, Vol. 7, no 11, 1111-1116 p.Article in journal (Refereed) Published
Abstract [en]

Inter-helix hydrogen bonding involving asparagine (Asn, N), glutamine (Gin, Q), aspartic acid (Asp, D) or glutamic acid (Glu, E) can drive efficient di- or trimerization of transmembrane helices in detergent micelles and lipid bilayers. Likewise, Asn-Asn and Asp-Asp pairs can promote the formation of helical hairpins during translocon-mediated membrane protein assembly in the endoplasmic reticulum. By in vitro translation of model integral membrane protein constructs in the presence of rough microsomes, we show that Asn- or Asp-mediated interactions with a neighbouring transmembrane helix can enhance the membrane insertion efficiency of a marginally hydrophobic transmembrane segment. Our observations suggest that inter-helix hydrogen bonds can form during Sec61 translocon-assisted insertion and thus could be important for membrane protein assembly.

Place, publisher, year, edition, pages
2006. Vol. 7, no 11, 1111-1116 p.
Keyword [en]
endoplasmic reticulum, helix-helix interaction, membrane protein assembly, Sec61, transmembrane helix
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:su:diva-25790DOI: 10.1038/sj.embor.7400818ISI: 000242279500012OAI: oai:DiVA.org:su-25790DiVA: diva2:200522
Available from: 2009-03-19 Created: 2009-02-20 Last updated: 2016-02-23Bibliographically approved
In thesis
1. Integration and topology of membrane proteins
Open this publication in new window or tab >>Integration and topology of membrane proteins
2009 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

Membrane proteins comprise around 20-30% of most proteomes. They play important roles in most biochemical pathways. All receptors and ion channels are membrane proteins, which make them attractive targets for drug design. Membrane proteins insert and fold co-translationally into the endoplasmic reticular membrane of eukaryotic cells. The protein-conducting channel that inserts the protein into the membrane is called Sec61 translocon, which is a hetero-oligomeric channel that allows transmembrane segments to insert laterally into the lipid bilayer. The focus of this thesis is how the translocon recognizes the transmembrane helices and integrates them into the membrane.

We have investigated the sequence requirements for the translocon-mediated integration of a transmembrane α-helix into the ER by challenging the Sec61 translocon with designed polypeptide segments in an in vitro expression system that allows a quantitative assessment of membrane insertion efficiency. Our studies suggest that helices might interact with each other already during the membrane-insertion step, possibly forming helical hairpins that partition into the membrane as a single unit. Further, the insertion efficiency for Nin-Cout vs. Nout-Cin transmembrane helices and the integration efficiency of Alzheimer’s Aβ-peptide fragments has been investigated.

Finally, detailed topology mapping was performed on two biologically interesting proteins with unknown topology, the human seipin protein and Drosophila melanogaster odorant receptor OR83b.

Place, publisher, year, edition, pages
Stockholm: Institutionen för biokemi och biofysik, 2009. 53 p.
Keyword
insertion, Sec61, translocation
National Category
Biochemistry and Molecular Biology
Research subject
Biochemistry
Identifiers
urn:nbn:se:su:diva-8575 (URN)978-91-7155-827-5 (ISBN)
Public defence
2009-04-09, Magnélisalen, Kemiska övningslaboratoriet, Svante Arrhenius väg 12 A, Stockholm, 10:00 (English)
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Available from: 2009-03-12 Created: 2009-02-20 Last updated: 2016-02-23Bibliographically approved

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