Asn- and Asp-mediated interactions between transmembrane helices during translocon-mediated membrane protein assembly
2006 (English)In: EMBO reports, ISSN 1469-221X, Vol. 7, no 11, 1111-1116 p.Article in journal (Refereed) Published
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.
endoplasmic reticulum, helix-helix interaction, membrane protein assembly, Sec61, transmembrane helix
Biochemistry and Molecular Biology
IdentifiersURN: urn:nbn:se:su:diva-25790DOI: 10.1038/sj.embor.7400818ISI: 000242279500012OAI: oai:DiVA.org:su-25790DiVA: diva2:200522