Recognition of transmembrane helices by the endoplasmic reticulum translocon
By T. Hessa, Hyun Kim, Karl Bihlmaier, C. Lundin, J. Boekel, H. Andersson, I. Nilsson, S. White, G. von Heijne. Nature, 2005
996 citations recorded by the source corpus.
Membrane proteins depend on complex translocation machineries for insertion into target membranes. Although it has long been known that an abundance of nonpolar residues in transmembrane helices is the principal criterion for membrane insertion, the specific sequence-coding for transmembrane helices has not been identified. By challenging the endoplasmic reticulum Sec61 translocon with an extensive set of designed polypeptide segments, we have determined the basic features of this code, including a ‘biological’ hydrophobicity scale. We find that membrane insertion depends strongly on the position of polar residues within transmembrane segments, adding a new dimension to the problem of predicting transmembrane helices from amino acid sequences. Our results indicate that direct protein–lipid interactions are critical during translocon-mediated membrane insertion.
Subfields: Genetics, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/4d171a0336310d93ea49df74f5e7c1dffe1953c3
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Citations in the corpus
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- De novo protein design, a retrospective (2020, background): “The features required for insertion are well understood from elegant studies of von Heijne, White, and others who examined the sequencedependence of helix insertion into membranes via the translocon (Hessa et al., 2005; White and von Heijne, 2005, 2008).”
- Topology Prediction of α-Helical Transmembrane Proteins (2016, methodology): “• Experimental-based scales were developed by Hopp [77], Goldman [78], Wimley [79], Hessa [7] and Moon [72] and are experimentally based.”
- A structural model of the active ribosome-bound membrane protein insertase YidC (2014, background): “This knowledge can be exploited to predict TM segments based on the hydrophobicity distribution of the primary amino acid sequence (Hessa et al., 2005) which will be located in the lipid bilayer.”
- Membrane-protein topology (2006, background): “, and the capability of the different amino acids to promote or reduce the insertion of model hydrophobic segments into the ER membran”