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Asn- and Asp-mediated interactions between transmembrane helices during translocon-mediated membrane protein assembly.

Authors :
Meindl-Beinker NM
Lundin C
Nilsson I
White SH
von Heijne G
Source :
EMBO reports [EMBO Rep] 2006 Nov; Vol. 7 (11), pp. 1111-6. Date of Electronic Publication: 2006 Sep 29.
Publication Year :
2006

Abstract

Inter-helix hydrogen bonding involving asparagine (Asn, N), glutamine (Gln, 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.

Details

Language :
English
ISSN :
1469-221X
Volume :
7
Issue :
11
Database :
MEDLINE
Journal :
EMBO reports
Publication Type :
Academic Journal
Accession number :
17008929
Full Text :
https://doi.org/10.1038/sj.embor.7400818