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Asn- and Asp-mediated interactions between transmembrane helices during translocon-mediated membrane protein assembly.
- 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.
- Subjects :
- Amino Acid Sequence
Animals
Dimerization
Dogs
Hydrogen Bonding
Membrane Proteins genetics
Models, Biological
Molecular Sequence Data
Pancreas enzymology
Peptide Hydrolases genetics
Protein Structure, Secondary
Asparagine chemistry
Aspartic Acid chemistry
Membrane Proteins metabolism
Peptide Hydrolases chemistry
Protein Biosynthesis
Subjects
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